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(Received for publication, May 1, 1997, and in revised form, July 31, 1997)
From the Department of Biochemistry, University of Leicester,
Leicester LE1 7RH, United Kingdom and the We have determined the high resolution crystal
structure of the I domain from the
Volume 272, Number 45,
Issue of November 7, 1997
pp. 28512-28517
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Crystal Structure of the I Domain from Integrin
2
1
,
and
Division of
Infectious Diseases, Dana-Farber Cancer Institute,
Boston, Massachusetts 02115
-subunit of the integrin
2
1, a cell surface adhesion receptor for collagen and the human
pathogen echovirus-1. The domain, as expected, adopts the
dinucleotide-binding fold, and contains a metal
ion-dependent adhesion site motif with bound Mg2+ at the top of the -sheet. Comparison with the
crystal structures of the leukocyte integrin I domains reveals a new
helix (the C-helix) protruding from the metal ion-dependent
adhesion site face of the domain which creates a groove centered on the
magnesium ion. Modeling of a collagen triple helix into the groove
suggests that a glutamic acid side chain from collagen can coordinate
the metal ion, and that the C-helix insert is a major determinant of
binding specificity. The binding site for echovirus-1 maps to a
distinct surface of the 2-I domain (one edge of the -sheet),
consistent with data showing that virus and collagen binding occur by
different mechanisms. Comparison with the homologous von Willebrand
factor A3 domain, which also binds collagen, suggests that the two
domains bind collagen in different ways.
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