5nl1: Difference between revisions

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'''Unreleased structure'''


The entry 5nl1 is ON HOLD
==Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512==
 
<StructureSection load='5nl1' size='340' side='right' caption='[[5nl1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5nl1]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NL1 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<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=5nl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nl1 OCA], [http://pdbe.org/5nl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nl1 RCSB], [http://www.ebi.ac.uk/pdbsum/5nl1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nl1 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [[http://www.uniprot.org/uniprot/IPAA_SHIFL IPAA_SHIFL]] Rapidly associates with the first 265 amino acids of vinculin after bacteria-cell contact. This interaction is critical for efficient Shigella uptake. IpaA acts as a potent activator of vinculin and increase its ability to interact with F-actin. The complex IpaA-vinculin induces F-actin depolymerization along with the occasional formation of actin filament bundles.<ref>PMID:9184218</ref> <ref>PMID:10545097</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bou-Nader, C]]
[[Category: Fontecave, M]]
[[Category: Nhieu, G Tran Van]]
[[Category: Pecqueur, L]]
[[Category: Valencia-Gallardo, C]]
[[Category: Structural protein]]

Revision as of 08:20, 16 May 2018

Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512

Structural highlights

5nl1 is a 12 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [IPAA_SHIFL] Rapidly associates with the first 265 amino acids of vinculin after bacteria-cell contact. This interaction is critical for efficient Shigella uptake. IpaA acts as a potent activator of vinculin and increase its ability to interact with F-actin. The complex IpaA-vinculin induces F-actin depolymerization along with the occasional formation of actin filament bundles.[1] [2]

References

  1. Tran Van Nhieu G, Ben-Ze'ev A, Sansonetti PJ. Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin. EMBO J. 1997 May 15;16(10):2717-29. PMID:9184218 doi:10.1093/emboj/16.10.2717
  2. Bourdet-Sicard R, Rudiger M, Jockusch BM, Gounon P, Sansonetti PJ, Nhieu GT. Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization. EMBO J. 1999 Nov 1;18(21):5853-62. PMID:10545097 doi:10.1093/emboj/18.21.5853

5nl1, resolution 2.50Å

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