3fyq: Difference between revisions
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==Structure of Drosophila melanogaster talin IBS2 domain (residues 1981-2168)== | ==Structure of Drosophila melanogaster talin IBS2 domain (residues 1981-2168)== | ||
<StructureSection load='3fyq' size='340' side='right' caption='[[3fyq]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3fyq' size='340' side='right'caption='[[3fyq]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fyq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3fyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FYQ FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rhea, CG6831, Dmel_CG6831 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rhea, CG6831, Dmel_CG6831 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyq OCA], [https://pdbe.org/3fyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fyq RCSB], [https://www.ebi.ac.uk/pdbsum/3fyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Cheung, T Y.S]] | [[Category: Cheung, T Y.S]] | ||
[[Category: Fairchild, M J]] | [[Category: Fairchild, M J]] | ||
Revision as of 10:51, 9 March 2022
Structure of Drosophila melanogaster talin IBS2 domain (residues 1981-2168)Structure of Drosophila melanogaster talin IBS2 domain (residues 1981-2168)
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIntegrins are transmembrane receptors that mediate cell adhesion to the extracellular matrix and play essential roles in tissue development and maintenance. The cytoplasmic segment of integrin associates with talin, a large intracellular protein that links integrin to the actin cytoskeleton. Binding of talin via an integrin binding segment (IBS1) results in large conformational changes in the extracellular portion of integrin, which modulates the affinity of integrins for their extracellular matrix ligands. However, integrin binding also requires a second segment of talin (IBS2). Despite detailed descriptions of the integrin-IBS1 binding, the molecular determinants that drive the integrin-IBS2 association are poorly understood. Here, we describe the crystal structure of the talin IBS2 domain, which forms a five-helix bundle. The large structural homology with a vinculin binding domain hints at an ancient gene duplication and suggests that helix 4 may bind to vinculin if the bundle is unfolded. Mapping previous mutations on the surface highlights a likely binding interface for integrin. Crystal structure of the talin integrin binding domain 2.,Cheung TY, Fairchild MJ, Zarivach R, Tanentzapf G, Van Petegem F J Mol Biol. 2009 Apr 10;387(4):787-93. PMID:19340939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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