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==Crystal structure of the SH3 domain from IRSp53 (BAIAP2)==
==Crystal structure of the SH3 domain from IRSp53 (BAIAP2)==
<StructureSection load='3rnj' size='340' side='right' caption='[[3rnj]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3rnj' size='340' side='right'caption='[[3rnj]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3rnj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RNJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3rnj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RNJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAIAP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAIAP2 ([https://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=3rnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rnj OCA], [http://pdbe.org/3rnj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rnj RCSB], [http://www.ebi.ac.uk/pdbsum/3rnj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rnj ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rnj OCA], [https://pdbe.org/3rnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rnj RCSB], [https://www.ebi.ac.uk/pdbsum/3rnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rnj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>   
[[https://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>   
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Barilari, M]]
[[Category: Barilari, M]]

Revision as of 13:18, 22 June 2022

Crystal structure of the SH3 domain from IRSp53 (BAIAP2)Crystal structure of the SH3 domain from IRSp53 (BAIAP2)

Structural highlights

3rnj is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:BAIAP2 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2] [3] [4]

References

  1. ↑ Miki H, Yamaguchi H, Suetsugu S, Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. PMID:11130076 doi:http://dx.doi.org/10.1038/35047107
  2. ↑ Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A. Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. Curr Biol. 2001 Oct 30;11(21):1645-55. PMID:11696321
  3. ↑ Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N. A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J Biol Chem. 2004 Apr 9;279(15):14929-36. Epub 2004 Jan 29. PMID:14752106 doi:http://dx.doi.org/10.1074/jbc.M309408200
  4. ↑ Vingadassalom D, Kazlauskas A, Skehan B, Cheng HC, Magoun L, Robbins D, Rosen MK, Saksela K, Leong JM. Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation. Proc Natl Acad Sci U S A. 2009 Apr 21;106(16):6754-9. doi:, 10.1073/pnas.0809131106. Epub 2009 Apr 6. PMID:19366662 doi:10.1073/pnas.0809131106

3rnj, resolution 1.50Å

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