6bd2: Difference between revisions

Revision as of 05:51, 24 October 2018

Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366

Structural highlights

6bd2 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	1PE, EDO, PEG, PG4, PGE
NonStd Res:	SEP, TPO
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[1433T_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.^[1] [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.^[2] ^[3] ^[4] ^[5]

References

↑ Sato S, Fujita N, Tsuruo T. Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3. J Biol Chem. 2002 Oct 18;277(42):39360-7. Epub 2002 Aug 12. PMID:12177059 doi:https://dx.doi.org/10.1074/jbc.M205141200
↑ 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] Sato S, Fujita N, Tsuruo T. Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3. J Biol Chem. 2002 Oct 18;277(42):39360-7. Epub 2002 Aug 12. PMID:12177059 doi:https://dx.doi.org/10.1074/jbc.M205141200

[2] 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

[3] 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

[4] 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

[5] 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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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6bd2 is ON HOLD  until Paper Publication
+==Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366==
+<StructureSection load='6bd2' size='340' side='right' caption='[[6bd2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-Authors: Kast, D.J., Dominguez, R.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6bd2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>
-Description: Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-[[Category: Kast, D.J]]
+<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=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [http://pdbe.org/6bd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [http://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref>  [[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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Dominguez, R]]
+[[Category: Kast, D J]]
+[[Category: Cell motility]]
+[[Category: Cytoskeleton regulation]]
+[[Category: Phosphate binding protein]]
+[[Category: Protein complex]]
+[[Category: Signaling protein]]

6bd2: Difference between revisions

Revision as of 05:51, 24 October 2018

Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366

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