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J. Biol. Chem., Vol. 276, Issue 43, 40055-40064, October 26, 2001
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From the The tetraspanin family of
membrane glycoproteins is involved in the regulation of cellular
development, proliferation, activation, and mobility. We have attempted
to predict the structural features of the large extracellular
domain of tetraspanins (EC2), which is very important in determining
their functional specificity. The tetraspanin EC2 is composed of
two subdomains: a conserved three-helix subdomain and a variable
secondary structure subdomain inserted within the conserved subdomain.
The occurrence of key disulphide bridges and other invariant residues
leads to a conserved relative topology of both subdomains and also
suggests a structural classification of tetraspanins. Using the CD81
EC2 structure as a template, the structures of two other EC2s
were predicted by homology modeling and indicate a conserved shape, in
which the variable subdomain is located at one side of the
structure. The conserved and variable subdomains might contain sites
that correspond, respectively, to common and specific interactions of
tetraspanins. The tetraspanin EC2 seems to correspond to a new
scheme of fold conservation/variability among proteins, namely the
insertion of a structurally variable subdomain within an otherwise
conserved fold.
Structure of the Tetraspanin Main Extracellular Domain
A PARTIALLY CONSERVED FOLD WITH A STRUCTURALLY
VARIABLE DOMAIN INSERTION*
,
Unité Mixte de Recherche,
7033 CNRS, Laboratoire de Physicochimie Biomoléculare et
Cellulaire, Université Paris 6, 4 Place Jussieu, 75005 Paris,
France and the § U332 INSERM, Institut Cochin de Genetique
Moleculaire, 22 Rue Méchain, 75014 Paris, France
*
This work was supported by grants from the Center National
de la Recherche Scientifique, The Institut National de la Santé et de la Recherche Médicale, and the Association pour la
Recherche sur le Cancer.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. Tel.:
33-1-40-51-6487; Fax: 33-1-40-51-6454; E-mail:
conjeaud@cochin.inserm.fr.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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