2ykt
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ykt' size='340' side='right' caption='[[2ykt]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='2ykt' size='340' side='right' caption='[[2ykt]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ykt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKT OCA]. <br> | + | <table><tr><td colspan='2'>[[2ykt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKT FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wdz|1wdz]], [[1y2o|1y2o]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wdz|1wdz]], [[1y2o|1y2o]]</td></tr> |
| - | <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=2ykt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykt RCSB], [http://www.ebi.ac.uk/pdbsum/2ykt PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | <table> | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref> [[http://www.uniprot.org/uniprot/C6UYL8_ECO5T C6UYL8_ECO5T]] Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.,de Groot JC, Schluter K, Carius Y, Quedenau C, Vingadassalom D, Faix J, Weiss SM, Reichelt J, Standfuss-Gabisch C, Lesser CF, Leong JM, Heinz DW, Bussow K, Stradal TE Structure. 2011 Sep 7;19(9):1294-306. PMID:21893288<ref>PMID:21893288</ref> | Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.,de Groot JC, Schluter K, Carius Y, Quedenau C, Vingadassalom D, Faix J, Weiss SM, Reichelt J, Standfuss-Gabisch C, Lesser CF, Leong JM, Heinz DW, Bussow K, Stradal TE Structure. 2011 Sep 7;19(9):1294-306. PMID:21893288<ref>PMID:21893288</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Buessow, K | + | [[Category: Buessow, K]] |
| - | [[Category: Carius, Y | + | [[Category: Carius, Y]] |
| - | [[Category: Faix, J | + | [[Category: Faix, J]] |
| - | [[Category: Groot, J C.De | + | [[Category: Groot, J C.De]] |
| - | [[Category: Heinz, D W | + | [[Category: Heinz, D W]] |
| - | [[Category: Leong, J M | + | [[Category: Leong, J M]] |
| - | [[Category: Lesser, C F | + | [[Category: Lesser, C F]] |
| - | [[Category: Quedenau, C | + | [[Category: Quedenau, C]] |
| - | [[Category: Reichelt, J | + | [[Category: Reichelt, J]] |
| - | [[Category: Schlueter, K | + | [[Category: Schlueter, K]] |
| - | [[Category: Standfuss-Gabisch, C | + | [[Category: Standfuss-Gabisch, C]] |
| - | [[Category: Stradal, T E.B | + | [[Category: Stradal, T E.B]] |
| - | [[Category: Vingadassalom, D | + | [[Category: Vingadassalom, D]] |
| - | [[Category: Weiss, S M | + | [[Category: Weiss, S M]] |
[[Category: Binding pocket]] | [[Category: Binding pocket]] | ||
[[Category: Npy motif]] | [[Category: Npy motif]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 13:31, 24 December 2014
CRYSTAL STRUCTURE OF THE I-BAR DOMAIN OF IRSP53 (BAIAP2) IN COMPLEX WITH AN EHEC DERIVED TIR PEPTIDE
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