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FEBS Lett. 2002 Feb 20;513(1):98-106.

Functional plasticity of CH domains.

Author information

1
Department of Cell Biology, Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg, Austria. mgimona@server1.imolbio.oeaw.ac.at

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.

PMID:
11911887
DOI:
10.1016/s0014-5793(01)03240-9
[Indexed for MEDLINE]
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