2jod
From Proteopedia
(New page: 200px<br /> <applet load="2jod" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jod" /> '''Pac1-Rshort N-terminal EC domain Pacap(6-38...) |
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'''Pac1-Rshort N-terminal EC domain Pacap(6-38) complex'''<br /> | '''Pac1-Rshort N-terminal EC domain Pacap(6-38) complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JOD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2JOD is a [http://en.wikipedia.org/wiki/Protein_complex 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]. |
==Reference== | ==Reference== | ||
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[[Category: protein/peptide complex]] | [[Category: protein/peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:11:51 2008'' |
Revision as of 13:11, 23 January 2008
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Pac1-Rshort N-terminal EC domain Pacap(6-38) complex
Overview
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.
About this Structure
2JOD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS., Sun C, Song D, Davis-Taber RA, Barrett LW, Scott VE, Richardson PL, Pereda-Lopez A, Uchic ME, Solomon LR, Lake MR, Walter KA, Hajduk PJ, Olejniczak ET, Proc Natl Acad Sci U S A. 2007 May 8;104(19):7875-80. Epub 2007 Apr 30. PMID:17470806
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