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1t01

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Revision as of 18:44, 24 December 2014

Vinculin complexed with the VBS1 helix from talin

Structural highlights

1t01 is a 2 chain structure with sequence from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1sj8, 1sj7
Gene:	VCL (Gallus gallus), TLN1, TLN (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VINC_CHICK] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.^[1] ^[2] ^[3] [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.

Evolutionary Conservation

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

Publication Abstract from PubMed

The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482-789. Talin 482-655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656-789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions.

Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle.,Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J EMBO J. 2004 Aug 4;23(15):2942-51. Epub 2004 Jul 22. PMID:15272303^[4]

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

References

↑ Zhang Z, Izaguirre G, Lin SY, Lee HY, Schaefer E, Haimovich B. The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading. Mol Biol Cell. 2004 Sep;15(9):4234-47. Epub 2004 Jun 30. PMID:15229287 doi:10.1091/mbc.E04-03-0264
↑ le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol. 2010 Jun 28;189(7):1107-15. doi: 10.1083/jcb.201001149. PMID:20584916 doi:10.1083/jcb.201001149
↑ Peng X, Cuff LE, Lawton CD, DeMali KA. Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci. 2010 Feb 15;123(Pt 4):567-77. doi: 10.1242/jcs.056432. Epub 2010 Jan , 19. PMID:20086044 doi:10.1242/jcs.056432
↑ Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J. Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. EMBO J. 2004 Aug 4;23(15):2942-51. Epub 2004 Jul 22. PMID:15272303 doi:10.1038/sj.emboj.7600285

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t01"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1t01]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T01 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sj8|1sj8]], [[1sj7|1sj7]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sj8|1sj8]], [[1sj7|1sj7]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]), TLN1, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]), TLN1, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t01 RCSB], [http://www.ebi.ac.uk/pdbsum/1t01 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=1t01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t01 RCSB], [http://www.ebi.ac.uk/pdbsum/1t01 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</ref>  [[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 38: @@
 [[Category: Gallus gallus]]
 [[Category: Mus musculus]]
-[[Category: Barsukov, I L.]]
+[[Category: Barsukov, I L]]
-[[Category: Critchley, D R.]]
+[[Category: Critchley, D R]]
-[[Category: Emsley, J.]]
+[[Category: Emsley, J]]
-[[Category: Gingras, A R.]]
+[[Category: Gingras, A R]]
-[[Category: Papagrigoriou, E.]]
+[[Category: Papagrigoriou, E]]
 [[Category: Cell adhesion]]
 [[Category: Five helix bundle]]
 [[Category: Structural protein]]

1t01

From Proteopedia

Revision as of 18:44, 24 December 2014

Vinculin complexed with the VBS1 helix from talin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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