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- W1550140963 abstract "The N-terminal approximately 440 aa of integrin alpha subunits contain seven sequence repeats. These are predicted here to fold into a beta-propeller domain. A homologous domain from the enzyme phosphatidylinositol phospholipase D is predicted to have the same fold. The domains contain seven four-stranded beta-sheets arranged in a torus around a pseudosymmetry axis. The trimeric G-protein beta subunit (G beta) appears to be the most closely related beta-propeller. Integrin ligands and a putative Mg2+ ion are predicted to bind to the upper face of the beta-propeller. This face binds substrates in beta-propeller enzymes and is used by the G protein beta subunit to bind the G protein alpha subunit. The integrin alpha subunit I domain, which is structurally homologous to the G protein alpha subunit, is tethered to the top of the beta-propeller domain by a hinge that may allow movement of the domains relative to one another. The Ca2+-binding motifs in integrin alpha subunits are on the lower face of the beta-propeller." @default.
- W1550140963 created "2016-06-24" @default.
- W1550140963 creator A5003615852 @default.
- W1550140963 date "1997-01-07" @default.
- W1550140963 modified "2023-10-02" @default.
- W1550140963 title "Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain" @default.
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- W1550140963 doi "https://doi.org/10.1073/pnas.94.1.65" @default.
- W1550140963 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/19237" @default.
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