1wdz: Difference between revisions

Latest revision as of 13:31, 13 March 2024

Crystal structure of RCB domain of IRSp53

Structural highlights

1wdz is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.63Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ 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:https://dx.doi.org/10.1038/35047107
↑ 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
↑ 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:https://dx.doi.org/10.1074/jbc.M309408200
↑ 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

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OCA

[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:https://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:https://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

[1]

[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='1wdz' size='340' side='right'caption='[[1wdz]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wdz]] is a 2 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=1WDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wdz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDZ FirstGlance]. <br>
-</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=1wdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdz OCA], [https://pdbe.org/1wdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdz RCSB], [https://www.ebi.ac.uk/pdbsum/1wdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdz ProSAT], [https://www.topsan.org/Proteins/RSGI/1wdz TOPSAN]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63&#8491;</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=1wdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdz OCA], [https://pdbe.org/1wdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdz RCSB], [https://www.ebi.ac.uk/pdbsum/1wdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdz ProSAT], [https://www.topsan.org/Proteins/RSGI/1wdz TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Murayama, K]]
+[[Category: Murayama K]]
-[[Category: Structural genomic]]
+[[Category: Seto A]]
-[[Category: Seto, A]]
+[[Category: Shirouzu M]]
-[[Category: Shirouzu, M]]
+[[Category: Suetsugu S]]
-[[Category: Suetsugu, S]]
+[[Category: Takenawa T]]
-[[Category: Takenawa, T]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
-[[Category: Cellular signaling protein]]
-[[Category: Rsgi]]
-[[Category: Signaling protein]]

1wdz: Difference between revisions

Latest revision as of 13:31, 13 March 2024

Crystal structure of RCB domain of IRSp53

Structural highlights

Function

Evolutionary Conservation

References

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