2m32: Difference between revisions
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==Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide== | |||
<StructureSection load='2m32' size='340' side='right' caption='[[2m32]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2m32]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M32 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2m32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m32 RCSB], [http://www.ebi.ac.uk/pdbsum/2m32 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> | |||
== | ==See Also== | ||
*[[Integrin|Integrin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Chin, Y | [[Category: Chin, Y]] | ||
[[Category: Emsley, J | [[Category: Emsley, J]] | ||
[[Category: Headey, S | [[Category: Headey, S]] | ||
[[Category: McEwan, P | [[Category: McEwan, P]] | ||
[[Category: Mohanty, B | [[Category: Mohanty, B]] | ||
[[Category: Mulhern, T | [[Category: Mulhern, T]] | ||
[[Category: Scanlon, M | [[Category: Scanlon, M]] | ||
[[Category: Simpson, J | [[Category: Simpson, J]] | ||
[[Category: Swarbrick, J | [[Category: Swarbrick, J]] | ||
[[Category: Alpha-1 integrin]] | [[Category: Alpha-1 integrin]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Glogen]] | [[Category: Glogen]] | ||
[[Category: I-domain]] | [[Category: I-domain]] | ||
Revision as of 19:43, 24 December 2014
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
Function[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. 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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