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| [[Image:2jod.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2jod.png|left|200px]] |
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| {{STRUCTURE_2jod| PDB=2jod | SCENE= }} | | {{STRUCTURE_2jod| PDB=2jod | SCENE= }} |
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| '''Pac1-Rshort N-terminal EC domain Pacap(6-38) complex'''
| | ===Pac1-Rshort N-terminal EC domain Pacap(6-38) complex=== |
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| ==Overview==
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| The pituitary adenylate cyclase-activating polypeptide (PACAP) receptor is a class II G protein-coupled receptor that contributes to many different cellular functions including neurotransmission, neuronal survival, and synaptic plasticity. The solution structure of the potent antagonist PACAP (residues 6'-38') complexed to the N-terminal extracellular (EC) domain of the human splice variant hPAC1-R-short (hPAC1-R(S)) was determined by NMR. The PACAP peptide adopts a helical conformation when bound to hPAC1-R(S) with a bend at residue A18' and makes extensive hydrophobic and electrostatic interactions along the exposed beta-sheet and interconnecting loops of the N-terminal EC domain. Mutagenesis data on both the peptide and the receptor delineate the critical interactions between the C terminus of the peptide and the C terminus of the EC domain that define the high affinity and specificity of hormone binding to hPAC1-R(S). These results present a structural basis for hPAC1-R(S) selectivity for PACAP versus the vasoactive intestinal peptide and also differentiate PACAP residues involved in binding to the N-terminal extracellular domain versus other parts of the full-length hPAC1-R(S) receptor. The structural, mutational, and binding data are consistent with a model for peptide binding in which the C terminus of the peptide hormone interacts almost exclusively with the N-terminal EC domain, whereas the central region makes contacts to both the N-terminal and other extracellular parts of the receptor, ultimately positioning the N terminus of the peptide to contact the transmembrane region and result in receptor activation. | | The line below this paragraph, {{ABSTRACT_PUBMED_17470806}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17470806 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17470806}} |
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| ==About this Structure== | | ==About this Structure== |
| 2JOD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOD OCA]. | | 2JOD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOD OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Walter, K A.]] | | [[Category: Walter, K A.]] |
| [[Category: Protein/peptide complex]] | | [[Category: Protein/peptide complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:06:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:34:29 2008'' |
