2kvp

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Solution Structure of the R10 Domain of TalinSolution Structure of the R10 Domain of Talin

Structural highlights

2kvp is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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
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