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J. Biol. Chem., Vol. 277, Issue 24, 21666-21674, June 14, 2002
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From the Department of Biology, University of Rome Tor Vergata, Via
della Ricerca Scientifica, Rome 00133, Italy
We have designed a repertoire of
107 different SH3 domains by grafting the residues
that are represented in the binding surfaces of natural SH3 domains
onto the scaffold of the human Abl-SH3 domain. This phage-displayed
library was screened by affinity selection for SH3 domains that bind to
the synthetic peptides, APTYPPPLPP and LSSRPLPTLPSP, which are peptide
ligands for the human Abl or Src SH3 domains, respectively. By
characterizing the isolates, we have observed that as few as two or
three amino acid substitutions lead to dramatic changes in recognition
specificity. We propose that the ability to shift recognition
specificity with a small number of amino acid replacements is an
important evolutionary characteristic of protein binding modules.
Furthermore, we have used the information obtained by these in
vitro evolution experiments to generate a scoring matrix that
evaluates the probability that any SH3 domain binds to the peptide
ligands for the Abl and Src SH3 domains. A table of predictions for the
28 SH3 domains of baker's yeast is presented.
In Vitro Evolution of Recognition Specificity
Mediated by SH3 Domains Reveals Target Recognition Rules*
, and
*
This work was supported by grants from Associazione Italiana
per la Ricerca sul Cancro, Target project biotechnology from CNR and
the European Union Biotechnology project.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.
Present address: Dept. of Physiology and Biochemistry, University
of Pisa, Via Carducci, 56010 Pisa, Italy.
§
To whom correspondence should be addressed. Tel.: 39-06-7259-4315;
Fax: 39-06-2023-500; E-mail: cesareni@uniroma2.it.
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