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Structure and distribution of modules in extracellular proteins

Published online by Cambridge University Press:  17 March 2009

Peer Bork ,
A. Kristina Downing ,
Bruno Kieffer  and
Iain D. Campbell
Peer Bork
Affiliation:
Max-Delbrück-Center for Molecular Medicine, 13125 Berlin-Buch, Germany and European Molecular Biology Laboratory, 69117 Heidelberg, Germany
A. Kristina Downing
Affiliation:
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Bruno Kieffer
Affiliation:
Groupe de Cancerogenese, IBMC de CNRS, 75084 Strasbourg, France
Iain D. Campbell
Affiliation:
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
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Extract

It has become standard practice to compare new amino-acid and nucleotide sequences with existing ones in the rapidly growing sequence databases. This has led to the recurring identification of certain sequence patterns, usually corresponding to less than 300 amino-acids in length. Many of these identifiable sequence regions have been shown to fold up to form a ‘domain’ structure; they are often called protein ‘modules’ (see definitions below). Proteins that contain such modules are widely distributed in biology, but they are particularly common in extracellular proteins.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 29 , Issue 2 , May 1996 , pp. 119 - 167
Copyright
Copyright © Cambridge University Press 1996

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