title: The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.
abstract: Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.
authors.affiliation: Department of Biochemistry, University of Leicester, Leicester, UK.
authors.forename: Benjamin T
authors.initials: BT
authors.lastname: Goult
authors.forename: Alexandre R
authors.initials: AR
authors.lastname: Gingras
authors.forename: Neil
authors.initials: N
authors.lastname: Bate
authors.forename: Igor L
authors.initials: IL
authors.lastname: Barsukov
authors.forename: David R
authors.initials: DR
authors.lastname: Critchley
authors.forename: Gordon C K
authors.initials: GC
authors.lastname: Roberts
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D003599:Cytoskeleton / Q000378:metabolism; D016023:Integrins / Q000378:metabolism; D051379:Mice; D011485:Protein Binding / Q000235:genetics; D017433:Protein Structure, Secondary / Q000235:genetics; D016608:Talin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016596:Vinculin / Q000378:metabolism*
chemical_list: D000199:Actins; D016023:Integrins; D016608:Talin; D016596:Vinculin
references.citation: Biomol NMR Assign. 2008 Jun;2(1):17-9
references.pmid: 19636914
references.citation: Biochemistry. 2006 Feb 14;45(6):1805-17
references.pmid: 16460027
references.citation: PLoS Comput Biol. 2008 Feb;4(2):e24
references.pmid: 18282082
references.citation: J Biomech. 2007;40(9):2096-106
references.pmid: 17544431
references.citation: J Mol Biol. 2008 Sep 26;382(1):112-26
references.pmid: 18638481
references.citation: J Biol Chem. 2005 Nov 4;280(44):37217-24
references.pmid: 16135522
references.citation: J Biol Chem. 2006 Mar 17;281(11):7458-67
references.pmid: 16407302
references.citation: Biophys Rev. 2009 Jul;1(2):61-69
references.pmid: 19655048
references.citation: J Biol Chem. 2009 Mar 27;284(13):8866-76
references.pmid: 19176533
references.citation: J Cell Sci. 1996 Nov;109 ( Pt 11):2715-26
references.pmid: 8937989
references.citation: J Biol Chem. 2009 May 29;284(22):15097-106
references.pmid: 19297334
references.citation: Biophys J. 2008 Aug;95(4):2027-36
references.pmid: 18408041
references.citation: Biochemistry. 2007 Sep 25;46(38):10886-98
references.pmid: 17722883
references.citation: J Mol Biol. 1995 Apr 7;247(4):536-40
references.pmid: 7723011
references.citation: Structure. 2005 Jan;13(1):65-74
references.pmid: 15642262
references.citation: Proteins. 2005 Jun 1;59(4):687-96
references.pmid: 15815974
references.citation: EMBO J. 2008 Jan 23;27(2):458-69
references.pmid: 18157087
references.citation: Annu Rev Biophys. 2009;38:235-54
references.pmid: 19416068
references.citation: EMBO J. 2004 Aug 4;23(15):2942-51
references.pmid: 15272303
references.citation: Science. 2009 Jan 30;323(5914):638-41
references.pmid: 19179532
references.citation: J Biol Chem. 2010 Sep 17;285(38):29577-87
references.pmid: 20610383