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2m32
From Proteopedia
(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> | |
| - | ==Function== | + | </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. | [[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 16:43, 24 December 2014
Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide
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Categories: Human | Chin, Y | Emsley, J | Headey, S | McEwan, P | Mohanty, B | Mulhern, T | Scanlon, M | Simpson, J | Swarbrick, J | Alpha-1 integrin | Cell adhesion | Glogen | I-domain
