3n94: Difference between revisions
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[[ | ==Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain== | ||
<StructureSection load='3n94' size='340' side='right' caption='[[3n94]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3n94]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N94 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994, ADCYAP1R1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n94 RCSB], [http://www.ebi.ac.uk/pdbsum/3n94 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pituitary adenylate cyclase activating polypeptide (PACAP) is a member of the PACAP/glucagon family of peptide hormones, which controls many physiological functions in the immune, nervous, endocrine, and muscular systems. It activates adenylate cyclase by binding to its receptor, PAC1R, a member of class B G-protein coupled receptors (GPCR). Crystal structures of a number of Class B GPCR extracellular domains (ECD) bound to their respective peptide hormones have revealed a consensus mechanism of hormone binding. However, the mechanism of how PACAP binds to its receptor remains controversial as an NMR structure of the PAC1R ECD/PACAP complex reveals a different topology of the ECD and a distinct mode of ligand recognition. Here we report a 1.9 A crystal structure of the PAC1R ECD, which adopts the same fold as commonly observed for other members of Class B GPCR. Binding studies and cell-based assays with alanine-scanned peptides and mutated receptor support a model that PAC1R uses the same conserved fold of Class B GPCR ECD for PACAP binding, thus unifying the consensus mechanism of hormone binding for this family of receptors. | |||
Crystal Structure of the PAC1R Extracellular Domain Unifies a Consensus Fold for Hormone Recognition by Class B G-Protein Coupled Receptors.,Kumar S, Pioszak A, Zhang C, Swaminathan K, Xu HE PLoS One. 2011;6(5):e19682. Epub 2011 May 19. PMID:21625560<ref>PMID:21625560</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hormone|Hormone]] | *[[Hormone|Hormone]] | ||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Kumar, S | [[Category: Kumar, S]] | ||
[[Category: Pioszak, A A | [[Category: Pioszak, A A]] | ||
[[Category: Swaminathan, K | [[Category: Swaminathan, K]] | ||
[[Category: Xu, H E | [[Category: Xu, H E]] | ||
[[Category: G-protein coupled receptor]] | [[Category: G-protein coupled receptor]] | ||
[[Category: Mbp fusion protein]] | [[Category: Mbp fusion protein]] | ||
[[Category: Membrane receptor]] | [[Category: Membrane receptor]] | ||
[[Category: Peptide hormone receptor]] | [[Category: Peptide hormone receptor]] | ||
Revision as of 09:58, 9 December 2014
Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain
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