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J. Biol. Chem., Vol. 276, Issue 26, 24160-24169, June 29, 2001
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From the Epidermal growth factor-like (EGF) and
short consensus repeat (SCR) domains are commonly found in cell surface
and soluble proteins that mediate specific protein-protein recognition
events. Unlike the immunoglobulin (Ig) superfamily, very little
is known about the general properties of intermolecular interactions
encoded by these common modules, and in particular, how specificity of binding is achieved. We have dissected the binding of CD97 (a member of
the EGF-TM7 family) to the complement regulator CD55, two cell surface
modular proteins that contain EGF and SCR domains, respectively. We
demonstrate that the interaction is mediated solely by these domains
and is characterized by a low affinity (86 µM) and
rapid off-rate (at least 0.6 s
Molecular Analysis of the Epidermal Growth
Factor-like Short Consensus Repeat Domain-mediated Protein-Protein
Interactions
DISSECTION OF THE CD97-CD55 COMPLEX*
§,¶,
,,,§§,
Sir William Dunn School of Pathology, South
Parks Road, Oxford, United Kingdom OX1 3RE, the Laboratory of
Molecular Biophysics, and the ** Division of Molecular and Cellular
Biochemistry, Department of Biochemistry, University of Oxford, South
Parks Road, Oxford, United Kingdom OX1 3QU; the
Institute of Biomedical and Life Sciences,
University of Glasgow, Church Street, Glasgow, United Kingdom G12 8QQ;
and the ¶¶ Department of Clinical Sciences, Institute of
Liver Studies, King's College Hospital, Bessemer Rd, London, United
Kingdom WC2R 2LS
1). The interaction is
Ca2+ -dependent but is unaffected by
glycosylation of the EGF domains. Using biotinylated multimerized
peptides in cell binding assays and surface plasmon resonance, we show
that a CD97-related EGF-TM7 molecule (termed EMR2), differing by only
three amino acids within the EGF domains, binds CD55 with a
KD at least an order of magnitude weaker than that
of CD97. These results suggest that low affinity cell-cell
interactions may be a general feature of highly expressed cell surface
proteins and that specificity of SCR-EGF binding can be finely tuned by
a small number of amino acid changes on the EGF module surface.
*
This work was supported in part by the Wellcome Trust (to
P. H., V. K., and Y. C. and for the BIAcore 2000) and the Arthritis Research Campaign (to S. L.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Biochemistry, University of Oxford, Oxford OX1 3QU. Tel.: 44 (0)1865 275181; Fax: 44 (0)1865 275182; E-mail: susan@biop.ox.ac.uk.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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