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The glycine-rich sequence of protein kinases: a multifunctional element

Authors
Journal
Trends in Biochemical Sciences
0968-0004
Publisher
Elsevier
Publication Date
Volume
19
Issue
5
Identifiers
DOI: 10.1016/0968-0004(94)90022-1
Disciplines
  • Biology

Abstract

Abstract Evolution favours the use of glycine-rich loops for nucleotide binding in proteins. In the large family of protein kinases, the catalytic domain of which has one of the higest degrees of conservation among all known proteins, the structure of the nucleotide-binding site differs from classical folds. We are now beginning to understand the multiple functional roles of the glycine-rich sequence in protein kinases and some of the structural constraints leading to its conservation.

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