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.

1zvz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844

Structural highlights

1zvz is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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. Three vinculin binding sites (VBS1-3) have previously been identified in the talin rod using a yeast two-hybrid assay. To extend these studies, we spot-synthesized a series of peptides spanning all the alpha-helical regions predicted for the talin rod and identified eight additional VBSs, two of which overlap key functional regions of the rod, including the integrin binding site and C-terminal actin binding site. The talin VBS alpha-helices bind to a hydrophobic cleft in the N-terminal vinculin Vd1 domain. We have defined the specificity of this interaction by spot-synthesizing a series of 25-mer talin VBS1 peptides containing substitutions with all the commonly occurring amino acids. The consensus for recognition is LXXAAXXVAXX- VXXLIXXA with distinct classes of hydrophobic side chains at positions 1, 4, 5, 8, 9, 12, 15, and 16 required for vinculin binding. Positions 1, 8, 12, 15, and 16 require an aliphatic residue and will not tolerate alanine, whereas positions 4, 5, and 9 are less restrictive. These preferences are common to all 11 VBS sequences with a minor variation occurring in one case. A crystal structure of this variant VBS peptide in complex with the vinculin Vd1 domain reveals a subtly different mode of vinculin binding.

Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod.,Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, Critchley DR, Emsley J J Biol Chem. 2005 Nov 4;280(44):37217-24. Epub 2005 Aug 30. PMID:16135522^[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
↑ Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, Critchley DR, Emsley J. Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod. J Biol Chem. 2005 Nov 4;280(44):37217-24. Epub 2005 Aug 30. PMID:16135522 doi:10.1074/jbc.M508060200

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/1zvz"

@@ Line 1: / Line 1: @@
 ==Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844==
-<StructureSection load='1zvz' size='340' side='right' caption='[[1zvz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1zvz' size='340' side='right'caption='[[1zvz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zvz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZVZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zvz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZVZ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCL, VINC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</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]] 1.8&#8491;</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=1zvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zvz RCSB], [http://www.ebi.ac.uk/pdbsum/1zvz PDBsum]</span></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=1zvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvz OCA], [https://pdbe.org/1zvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zvz RCSB], [https://www.ebi.ac.uk/pdbsum/1zvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvz ProSAT]</span></td></tr>
 </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_CHICK TLN1_CHICK]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a high molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
+[https://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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zv/1zvz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zv/1zvz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zvz ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1zvz" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 37: @@
 </StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Barsukov, I L]]
+[[Category: Large Structures]]
-[[Category: Critchley, D R]]
+[[Category: Barsukov IL]]
-[[Category: Emsley, J]]
+[[Category: Critchley DR]]
-[[Category: Gingras, A R]]
+[[Category: Emsley J]]
-[[Category: Roberts, G C]]
+[[Category: Gingras AR]]
-[[Category: Ziegler, W H]]
+[[Category: Roberts GC]]
-[[Category: Complex]]
+[[Category: Ziegler WH]]
-[[Category: Protein binding]]
-[[Category: Talin]]
-[[Category: Vinculin]]

1zvz

From Proteopedia

Current revision

Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox