Structural highlights
Function
[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
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.
The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.,Goult BT, Gingras AR, Bate N, Barsukov IL, Critchley DR, Roberts GC FEBS Lett. 2010 Jun 3;584(11):2237-41. Epub 2010 Apr 20. PMID:20399778[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goult BT, Gingras AR, Bate N, Barsukov IL, Critchley DR, Roberts GC. The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site. FEBS Lett. 2010 Jun 3;584(11):2237-41. Epub 2010 Apr 20. PMID:20399778 doi:10.1016/j.febslet.2010.04.028
