2m32: Difference between revisions
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== | ==Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide== | ||
[[http://www.uniprot.org/uniprot/ITA1_HUMAN ITA1_HUMAN | <StructureSection load='2m32' size='340' side='right'caption='[[2m32]]' scene=''> | ||
== Structural highlights == | |||
<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" 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> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
We 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<ref>PMID:24187131</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2m32" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Integrin 3D structures|Integrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[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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