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(-) Description

Title :  NMR STRUCTURE OF THE INTRACELLULAR LOOP (I3) OF THE VASOPRESSIN V2 RECEPTOR (GPCR)
 
Authors :  G. Bellot, H. Demene
Date :  06 Nov 07  (Deposition) - 18 Nov 08  (Release) - 24 Feb 09  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
Keywords :  Protein, G-Protein Coupled Receptor, Glycoprotein, Lipoprotein, Membrane, Palmitate, Phosphorylation, Receptor, Transducer, Transmembrane, Membrane Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  G. Bellot, S. Granier, W. Bourguet, R. Seyer, R. Rahmeh, B. Mouillac, R. Pascal, C. Mendre, H. Demene
Structure Of The Third Intracellular Loop Of The Vasopressin V2 Receptor And Conformational Changes Upon Binding To Gc1Qr
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - VASOPRESSIN V2 RECEPTOR
    ChainsA
    EngineeredYES
    FragmentRESIDUES 225-273
    MutationYES
    Other DetailsSYNTHESIS UNDER A CYCLIZED FORM: THIO-ETHER BRIDGE BETWEEN THE C-TERMINAL CYSTEINE RESIDUE (CYC) AND THE N-TERMINAL GLYCINE WERE CONSTRUCTED
    Other Details - SourceTHE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SOURCE SEQUENCE IS NATURALLY FOUND IN RAT (V2 RAT RECEPTOR).
    SynonymRENAL-TYPE ARGININE VASOPRESSIN RECEPTOR, ANTIDIURETIC HORMONE RECEPTOR, AVPR V2
    SyntheticYES

 Structural Features

(-) Chains, Units

  
NMR Structure (20x)

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (4, 5)

NMR Structure (4, 5)
No.NameCountTypeFull Name
1CCS1Mod. Amino AcidCARBOXYMETHYLATED CYSTEINE
2DGN1Mod. Amino AcidD-GLUTAMINE
3NH21Mod. Amino AcidAMINO GROUP
4NLE2Mod. Amino AcidNORLEUCINE

(-) Sites  (1, 1)

NMR Structure (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLY A:1 , CCS A:51 , PHE A:229 , VAL A:270 , ARG A:271 , THR A:273BINDING SITE FOR RESIDUE NH2 A 52

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2JX4)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2JX4)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2JX4)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2JX4)

(-) Exons   (0, 0)

(no "Exon" information available for 2JX4)

(-) Sequences/Alignments

NMR Structure
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:52
 aligned with V2R_RAT | Q00788 from UniProtKB/Swiss-Prot  Length:371

    Alignment length:97
                                   197       207       217       227       237       247       257       267       277       
              V2R_RAT   188 GVFDCWARFAEPWGLRAYVTWIALMVFVAPALGIAACQVLIFREIHASLVPGPSERAGRRRRGRRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCW 284
               SCOP domains ------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------7tm_1-2jx4A01 A:226-271                       ------------- Pfam domains
         Sec.struct. author .h------------------------------------hhhhhhhhhhhhhhhhhh.........hhhhhhhhhhhhhhhhhhhhh---------h. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------- Transcript
                 2jx4 A   1 Gx------------------------------------VLIFREIHASLVPGPSERAGRRRRGRRTGSPSEGAHVSAAlAKTVRlT---------cx  52
                            ||       -         -         -       227       237       247       257       267    ||   -     ||
                            ||                                  226                                     266-NLE ||        51-CCS
                            1|                                                                                272-NLE      52-NH2
                           225-DGN                                                                             273           

   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 2JX4)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2JX4)

(-) Pfam Domains  (1, 1)

NMR Structure
(-)
Clan: GPCR_A (90)

(-) Gene Ontology  (25, 25)

NMR Structure(hide GO term definitions)
Chain A   (V2R_RAT | Q00788)
molecular function
    GO:0004930    G-protein coupled receptor activity    Combining with an extracellular signal and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
    GO:0017046    peptide hormone binding    Interacting selectively and non-covalently with any peptide with hormonal activity in animals.
    GO:0004871    signal transducer activity    Conveys a signal across a cell to trigger a change in cell function or state. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response.
    GO:0005000    vasopressin receptor activity    Combining with vasopressin to initiate a change in cell activity.
biological process
    GO:0007186    G-protein coupled receptor signaling pathway    A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
    GO:0007249    I-kappaB kinase/NF-kappaB signaling    The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
    GO:0032870    cellular response to hormone stimulus    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus.
    GO:0032609    interferon-gamma production    The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon.
    GO:0035814    negative regulation of renal sodium excretion    Any process that decreases the amount of sodium excreted in urine over a unit of time.
    GO:0035811    negative regulation of urine volume    Any process that decreases the amount of urine excreted from the body over a unit of time.
    GO:0045777    positive regulation of blood pressure    Any process in which the force of blood traveling through the circulatory system is increased.
    GO:0008284    positive regulation of cell proliferation    Any process that activates or increases the rate or extent of cell proliferation.
    GO:0010628    positive regulation of gene expression    Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
    GO:0003084    positive regulation of systemic arterial blood pressure    The process that increases the force with which blood travels through the systemic arterial circulatory system.
    GO:0045907    positive regulation of vasoconstriction    Any process that activates or increases the frequency, rate or extent of vasoconstriction.
    GO:0001992    regulation of systemic arterial blood pressure by vasopressin    The regulation of blood pressure mediated by the signaling molecule vasopressin. Vasopressin is produced in the hypothalamus, and affects vasoconstriction, and renal water transport.
    GO:0034097    response to cytokine    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cytokine stimulus.
    GO:1901652    response to peptide    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a peptide stimulus.
    GO:0007165    signal transduction    The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
    GO:0021537    telencephalon development    The process whose specific outcome is the progression of the telencephalon over time, from its formation to the mature structure. The telencephalon is the paired anteriolateral division of the prosencephalon plus the lamina terminalis from which the olfactory lobes, cerebral cortex, and subcortical nuclei are derived.
cellular component
    GO:0016021    integral component of membrane    The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
    GO:0005887    integral component of plasma membrane    The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
    GO:0005622    intracellular    The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm.
    GO:0016020    membrane    A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
    GO:0005886    plasma membrane    The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

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