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A structure prediction for the ligand‐binding region of the integrin β subunit: evidence for the presence of a von Willebrand factor A domain
Author(s) -
Tuckwell Danny S,
Humphries Martin J
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01368-3
Subject(s) - von willebrand factor , integrin , protein subunit , receptor , ligand (biochemistry) , chemistry , binding site , microbiology and biotechnology , protein tertiary structure , binding domain , computational biology , biology , biophysics , biochemistry , immunology , gene , platelet
The integrins are a family of cell surface receptors that mediate biologically important adhesive interactions. Integrin‐ligand binding has been extensively studied because of the potential for the development of anti‐adhesive therapies, but the molecular basis of this interaction is still poorly understood. A conserved region near the N‐terminus of the β subunit appears to be of particular importance in ligand binding, but to date this domain has not been expressed in isolation. As a prelude to expression and potential structure determination, we have performed a detailed structure prediction for this region. Primary, secondary and tertiary structure analyses indicate that the region folds into a von Willebrand factor A‐domain, thereby potentially placing a previously characterised module at the centre of a key functional region.