3zdl
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[Image:3zdl.png|left|200px]] | ||
- | |||
{{STRUCTURE_3zdl| PDB=3zdl | SCENE= }} | {{STRUCTURE_3zdl| PDB=3zdl | SCENE= }} | ||
- | |||
===Vinculin head (1-258) in complex with a RIAM fragment=== | ===Vinculin head (1-258) in complex with a RIAM fragment=== | ||
- | |||
{{ABSTRACT_PUBMED_23389036}} | {{ABSTRACT_PUBMED_23389036}} | ||
+ | |||
+ | ==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/AB1IP_HUMAN AB1IP_HUMAN]] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.<ref>PMID:14530287</ref> <ref>PMID:15469846</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[3zdl]] 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=3ZDL OCA]. | [[3zdl]] 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=3ZDL OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <references group="xtra"/><references/> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Barsukov, I L.]] | [[Category: Barsukov, I L.]] |
Revision as of 21:41, 10 April 2013
Contents |
Vinculin head (1-258) in complex with a RIAM fragment
Template:ABSTRACT PUBMED 23389036
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] [AB1IP_HUMAN] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.[4] [5]
About this Structure
3zdl is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
- ↑ 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
- ↑ Inagaki T, Suzuki S, Miyamoto T, Takeda T, Yamashita K, Komatsu A, Yamauchi K, Hashizume K. The retinoic acid-responsive proline-rich protein is identified in promyeloleukemic HL-60 cells. J Biol Chem. 2003 Dec 19;278(51):51685-92. Epub 2003 Oct 6. PMID:14530287 doi:10.1074/jbc.M308016200
- ↑ Lafuente EM, van Puijenbroek AA, Krause M, Carman CV, Freeman GJ, Berezovskaya A, Constantine E, Springer TA, Gertler FB, Boussiotis VA. RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Dev Cell. 2004 Oct;7(4):585-95. PMID:15469846 doi:10.1016/j.devcel.2004.07.021