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

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 highest degrees of conservation among all known proteins, the structure of the nucleotide-binding site differs from classical folds...

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Bibliographic Details
Published in:	Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 19; no. 5; p. 201
Main Author:	Bossemeyer, D
Format:	Journal Article
Language:	English
Published:	England 01-05-1994
Subjects:	Amino Acid Sequence Binding Sites Catalysis Glycine Models, Molecular Molecular Sequence Data Molecular Structure Nucleotides - metabolism Protein Kinases - chemistry Substrate Specificity
Online Access:	Get more information
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Summary:	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 highest 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.
ISSN:	0968-0004
DOI:	10.1016/0968-0004(94)90022-1