1gea: Difference between revisions

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[[~~Image~~:1gea.~~png|left|200px~~]]

==RECEPTOR-BOUND CONFORMATION OF PACAP21==

== Structural highlights ==

<table><tr><td colspan='2'>[[1gea]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GEA FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYN:2,6-DIAMINO-HEXANOIC+ACID+AMIDE'>LYN</scene></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gea OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gea RCSB], [http://www.ebi.ac.uk/pdbsum/1gea PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Many peptide hormones elicit a wide array of physiological effects by binding to G-protein coupled receptors. We have determined the conformation of pituitary adenylate cyclase activating polypeptide, PACAP(1--21)NH(2), bound to a PACAP-specific receptor by NMR spectroscopy. Residues 3--7 form a unique beta-coil structure that is preceded by an N-terminal extended tail. This beta-coil creates a patch of hydrophobic residues that is important for receptor binding. In contrast, the C-terminal region (residues 8--21) forms an alpha-helix, similar to that in the micelle-bound PACAP. Thus, the conformational difference between PACAP in the receptor-bound and the micelle-bound states is limited to the N-terminal seven residues. This observation is consistent with the two-step ligand transportation model in which PACAP first binds to the membrane nonspecifically and then diffuses two-dimensionally in search of its receptor; a conformational change at the N-terminal region then allows specific interactions between the ligand and the receptor.

~~{{STRUCTURE_1gea| PDB=1gea | SCENE= }}~~

Conformation of a peptide ligand bound to its G-protein coupled receptor.,Inooka H, Ohtaki T, Kitahara O, Ikegami T, Endo S, Kitada C, Ogi K, Onda H, Fujino M, Shirakawa M Nat Struct Biol. 2001 Feb;8(2):161-5. PMID:11175907<ref>PMID:11175907</ref>

~~===RECEPTOR-BOUND CONFORMATION OF PACAP21===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_11175907}}~~

== References ==

==~~About this Structure~~==

__TOC__

~~[[1gea]] is a 1 chain structure. Full experimental information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=1GEA OCA].~~

</StructureSection>

[[Category: Endo, S.]]

[[Category: Fujino, M.]]

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@@ Line 1: / Line 1: @@
-[[Image:1gea.png|left|200px]]
+==RECEPTOR-BOUND CONFORMATION OF PACAP21==
+<StructureSection load='1gea' size='340' side='right' caption='[[1gea]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gea]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GEA FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYN:2,6-DIAMINO-HEXANOIC+ACID+AMIDE'>LYN</scene></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gea OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gea RCSB], [http://www.ebi.ac.uk/pdbsum/1gea PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Many peptide hormones elicit a wide array of physiological effects by binding to G-protein coupled receptors. We have determined the conformation of pituitary adenylate cyclase activating polypeptide, PACAP(1--21)NH(2), bound to a PACAP-specific receptor by NMR spectroscopy. Residues 3--7 form a unique beta-coil structure that is preceded by an N-terminal extended tail. This beta-coil creates a patch of hydrophobic residues that is important for receptor binding. In contrast, the C-terminal region (residues 8--21) forms an alpha-helix, similar to that in the micelle-bound PACAP. Thus, the conformational difference between PACAP in the receptor-bound and the micelle-bound states is limited to the N-terminal seven residues. This observation is consistent with the two-step ligand transportation model in which PACAP first binds to the membrane nonspecifically and then diffuses two-dimensionally in search of its receptor; a conformational change at the N-terminal region then allows specific interactions between the ligand and the receptor.
-{{STRUCTURE_1gea|  PDB=1gea  |  SCENE=  }}
+Conformation of a peptide ligand bound to its G-protein coupled receptor.,Inooka H, Ohtaki T, Kitahara O, Ikegami T, Endo S, Kitada C, Ogi K, Onda H, Fujino M, Shirakawa M Nat Struct Biol. 2001 Feb;8(2):161-5. PMID:11175907<ref>PMID:11175907</ref>
-===RECEPTOR-BOUND CONFORMATION OF PACAP21===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11175907}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1gea]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEA OCA].
+</StructureSection>
 [[Category: Endo, S.]]
 [[Category: Fujino, M.]]