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Cited by 418

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

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

Open access
Springer, Timothy A.·1997·Proceedings of the National Academy of Sciences

Abstract

The N-terminal ≈440 aa of integrin α subunits contain seven sequence repeats. These are predicted here to fold into a β-propeller domain. A homologous domain from the enzyme phosphatidylinositol phospholipase D is predicted to have the same fold. The domains contain seven four-stranded β-sheets arranged in a torus around a pseudosymmetry axis. The trimeric G-protein β subunit (G beta) appears to be the most closely related β-propeller. Integrin ligands and a putative Mg 2+ ion are predicted to bind to the upper face of the β-propeller. This face binds substrates in β-propeller enzymes and is used by the G protein β subunit to bind the G protein α subunit. The integrin α subunit I domain, which is structurally homologous to the G protein α subunit, is tethered to the top of the β-propeller domain by a hinge that may allow movement of the domains relative to one another. The Ca 2+ -binding motifs in integrin α subunits are on the lower face of the β-propeller.

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Metadata

Authors
Springer, T. A.
Venue
Proceedings of the National Academy of Sciences
Published
1997-01-07
Volume
94
Issue
1
Pages
65-72
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1550140963
Cited by
418
References
3
FWCI
18.01
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. https://app.cochat.ai/papers/10.1073/pnas.94.1.65
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Springer, T. A. (1997). Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.1.65

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