This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5fzt

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 18:00, 12 July 2016

The crystal structure of R7R8 in complex with a DLC1 fragment.

Structural highlights

5fzt is a 2 chain structure with sequence from Mus musculus. 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. [RHG07_HUMAN] Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Cell migration requires coordination between integrin-mediated cell adhesion to the extracellular matrix and force applied to adhesion sites. Talin plays a key role in coupling integrin receptors to the actomyosin contractile machinery, while deleted in liver cancer 1 (DLC1) is a Rho GAP that binds talin and regulates Rho, and therefore actomyosin contractility. We show that the LD motif of DLC1 forms a helix that binds to the four-helix bundle of the talin R8 domain in a canonical triple-helix arrangement. We demonstrate that the same R8 surface interacts with the paxillin LD1 and LD2 motifs. We identify key charged residues that stabilize the R8 interactions with LD motifs and demonstrate their importance in vitro and in cells. Our results suggest a network of competitive interactions in adhesion complexes that involve LD motifs, and identify mutations that can be used to analyze the biological roles of specific protein-protein interactions in cell migration.

LD Motif Recognition by Talin: Structure of the Talin-DLC1 Complex.,Zacharchenko T, Qian X, Goult BT, Jethwa D, Almeida TB, Ballestrem C, Critchley DR, Lowy DR, Barsukov IL Structure. 2016 May 31. pii: S0969-2126(16)30077-6. doi:, 10.1016/j.str.2016.04.016. PMID:27265849^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim TY, Healy KD, Der CJ, Sciaky N, Bang YJ, Juliano RL. Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration. J Biol Chem. 2008 Nov 21;283(47):32762-70. doi: 10.1074/jbc.M800617200. Epub 2008, Sep 11. PMID:18786931 doi:10.1074/jbc.M800617200
↑ Kawai K, Iwamae Y, Yamaga M, Kiyota M, Ishii H, Hirata H, Homma Y, Yagisawa H. Focal adhesion-localization of START-GAP1/DLC1 is essential for cell motility and morphology. Genes Cells. 2009 Feb;14(2):227-41. doi: 10.1111/j.1365-2443.2008.01265.x. Epub, 2008 Jan 15. PMID:19170769 doi:10.1111/j.1365-2443.2008.01265.x
↑ Erlmann P, Schmid S, Horenkamp FA, Geyer M, Pomorski TG, Olayioye MA. DLC1 activation requires lipid interaction through a polybasic region preceding the RhoGAP domain. Mol Biol Cell. 2009 Oct;20(20):4400-11. doi: 10.1091/mbc.E09-03-0247. Epub 2009, Aug 26. PMID:19710422 doi:10.1091/mbc.E09-03-0247
↑ Zacharchenko T, Qian X, Goult BT, Jethwa D, Almeida TB, Ballestrem C, Critchley DR, Lowy DR, Barsukov IL. LD Motif Recognition by Talin: Structure of the Talin-DLC1 Complex. Structure. 2016 May 31. pii: S0969-2126(16)30077-6. doi:, 10.1016/j.str.2016.04.016. PMID:27265849 doi:http://dx.doi.org/10.1016/j.str.2016.04.016

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fzt"

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[5fzt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FZT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></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=5fzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzt OCA], [http://pdbe.org/5fzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzt RCSB], [http://www.ebi.ac.uk/pdbsum/5fzt PDBsum]</span></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=5fzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzt OCA], [http://pdbe.org/5fzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzt RCSB], [http://www.ebi.ac.uk/pdbsum/5fzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzt ProSAT]</span></td></tr>
 </table>
 == Function ==

5fzt

From Proteopedia

Revision as of 18:00, 12 July 2016

The crystal structure of R7R8 in complex with a DLC1 fragment.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox