The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.
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.
Goult
Benjamin T
BT
Department of Biochemistry, University of Leicester, Leicester, UK.
Gingras
Alexandre R
AR
Bate
Neil
N
Barsukov
Igor L
IL
Critchley
David R
DR
Roberts
Gordon C K
GC
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*
D000199:Actins; D016023:Integrins; D016608:Talin; D016596:Vinculin
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