Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
- 7 January 1997
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (1), 65-72
- https://doi.org/10.1073/pnas.94.1.65
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.Keywords
This publication has 74 references indexed in Scilit:
- Determination of the Gene Sequence and the Three-dimensional Structure at 2.4 Å Resolution of Methanol Dehydrogenase fromMethylophilusW3A1Journal of Molecular Biology, 1996
- SCOP: A structural classification of proteins database for the investigation of sequences and structuresJournal of Molecular Biology, 1995
- The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β-sheet flanked by α-helices found in human ras-p21FEBS Letters, 1995
- An Alternatively Spliced Exon in the Extracellular Domain of the Human α6 Integrin Subunit-Functional Analysis of the α6 Integrin VariantsCell Adhesion and Communication, 1995
- The ancient regulatory-protein family of WD-repeat proteinsNature, 1994
- Comparative Protein Modelling by Satisfaction of Spatial RestraintsJournal of Molecular Biology, 1993
- Structural principles for the propeller assembly of β‐sheets: The preference for seven‐fold symmetryProteins-Structure Function and Bioinformatics, 1992
- A new approach to protein fold recognitionNature, 1992
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983