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Research Database PMU-SQQUID

Functional plasticity of CH domains.
Gimona, M; Djinovic-Carugo, K; Kranewitter, WJ; Winder, SJ;
FEBS Lett. 2002; 513(1): 98-106.
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PMU-Authors

Gimona Mario

Abstract

With the refinement of algorithms for the identification of distinct motifs from sequence databases, especially those using secondary structure predictions, new protein modules have been determined in recent years. Calponin homology (CH) domains were identified in a variety of proteins ranging from actin cross-linking to signaling and have been proposed to function either as autonomous actin binding motifs or serve a regulatory function. Despite the overall structural conservation of the unique CH domain fold, the individual modules display a quite striking functional variability. Analysis of the actopaxin/parvin protein family suggests the existence of novel (type 4 and type 5) CH domain families which require special attention, as they appear to be a good example for how CH domains may function as scaffolds for other functional motifs of different properties. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.


Useful keywords (using NLM MeSH Indexing)

Actinin/chemistry

Actinin/metabolism

Amino Acid Sequence

Animals

Binding Sites

Calcium-Binding Proteins/chemistry

Calcium-Binding Proteins/metabolism*

Dictyostelium/physiology

Microfilament Proteins

Molecular Sequence Data

Muscle Proteins/chemistry

Muscle Proteins/metabolism

Protein Binding

Protein Structure, Secondary

Sequence Alignment

Sequence Homology, Amino Acid

Spectrin/chemistry*

Spectrin/metabolism


Find related publications in this database (Keywords)

calponin
calponin homology domain
actin binding
actopaxin
paxillin binding
vav
alpha-actinin
dystrophin
fimbrin
spectrin
utrophin