NDLI: Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain

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Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain

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Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Springer, T. A.
Description	Author Affiliation: Springer TA ( Center for Blood Research and Harvard Medical School, Department of Pathology, Boston, MA 02115, USA.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Integrins Chemistry Protein Conformation Protein Folding Repetitive Sequences, Nucleic Acid Alternative Splicing Amino Acid Sequence Binding Sites Consensus Sequence Disulfides Ligands Models, Molecular Molecular Sequence Data Protein Structure, Secondary Sequence Alignment Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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