1y2o

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1y2o]] 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=1Y2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y2O FirstGlance]. <br>
<table><tr><td colspan='2'>[[1y2o]] 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=1Y2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y2O FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y2o RCSB], [http://www.ebi.ac.uk/pdbsum/1y2o PDBsum]</span></td></tr>
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<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=1y2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y2o RCSB], [http://www.ebi.ac.uk/pdbsum/1y2o PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bompard, G.]]
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[[Category: Bompard, G]]
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[[Category: Dafforn, T R.]]
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[[Category: Dafforn, T R]]
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[[Category: Futterer, K.]]
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[[Category: Futterer, K]]
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[[Category: Heung, M Y.]]
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[[Category: Heung, M Y]]
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[[Category: Machesky, L M.]]
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[[Category: Machesky, L M]]
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[[Category: Millard, T H.]]
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[[Category: Millard, T H]]
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[[Category: Scott, D J.]]
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[[Category: Scott, D J]]
[[Category: Actin bundling]]
[[Category: Actin bundling]]
[[Category: Cell motility]]
[[Category: Cell motility]]
[[Category: Filopodia]]
[[Category: Filopodia]]
[[Category: Signaling protein]]
[[Category: Signaling protein]]

Revision as of 20:12, 24 December 2014

Structure of N-terminal domain IRSp53/BAIAP2

1y2o, resolution 2.20Å

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