2m32: Difference between revisions
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==Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide== | ==Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide== | ||
<StructureSection load='2m32' size='340' side='right' caption='[[2m32 | <StructureSection load='2m32' size='340' side='right'caption='[[2m32]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m32]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2m32]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M32 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m32 OCA], [https://pdbe.org/2m32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m32 RCSB], [https://www.ebi.ac.uk/pdbsum/2m32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m32 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ITA1_HUMAN ITA1_HUMAN] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Integrin|Integrin]] | *[[Integrin 3D structures|Integrin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Chin | [[Category: Large Structures]] | ||
[[Category: Emsley | [[Category: Chin Y]] | ||
[[Category: Headey | [[Category: Emsley J]] | ||
[[Category: McEwan | [[Category: Headey S]] | ||
[[Category: Mohanty | [[Category: McEwan P]] | ||
[[Category: Mulhern | [[Category: Mohanty B]] | ||
[[Category: Scanlon | [[Category: Mulhern T]] | ||
[[Category: Simpson | [[Category: Scanlon M]] | ||
[[Category: Swarbrick | [[Category: Simpson J]] | ||
[[Category: Swarbrick J]] | |||
Latest revision as of 16:26, 22 February 2023
Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptideAlpha-1 integrin I-domain in complex with GLOGEN triple helical peptide
Structural highlights
FunctionITA1_HUMAN Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Publication Abstract from PubMedWe have determined the structure of the human integrin alpha1I domain bound to a triple-helical collagen peptide. The structure of the alpha1I-peptide complex was investigated using data from NMR, small angle x-ray scattering, and size exclusion chromatography that were used to generate and validate a model of the complex using the data-driven docking program, HADDOCK (High Ambiguity Driven Biomolecular Docking). The structure revealed that the alpha1I domain undergoes a major conformational change upon binding of the collagen peptide. This involves a large movement in the C-terminal helix of the alphaI domain that has been suggested to be the mechanism by which signals are propagated in the intact integrin receptor. The structure suggests a basis for the different binding selectivity observed for the alpha1I and alpha2I domains. Mutational data identify residues that contribute to the conformational change observed. Furthermore, small angle x-ray scattering data suggest that at low collagen peptide concentrations the complex exists in equilibrium between a 1:1 and 2:1 alpha1I-peptide complex. The structure of integrin alpha1I domain in complex with a collagen-mimetic peptide.,Chin YK, Headey SJ, Mohanty B, Patil R, McEwan PA, Swarbrick JD, Mulhern TD, Emsley J, Simpson JS, Scanlon MJ J Biol Chem. 2013 Dec 27;288(52):36796-809. doi: 10.1074/jbc.M113.480251. Epub, 2013 Nov 1. PMID:24187131[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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