Premium
Functional plasticity of CH domains
Author(s) -
Gimona Mario,
Djinovic-Carugo Kristina,
Kranewitter Wolfgang J.,
Winder Steven J.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03240-9
Subject(s) - calponin , computational biology , structural motif , functional analysis , biology , function (biology) , homology (biology) , sequence homology , protein domain , actin , peptide sequence , evolutionary biology , microbiology and biotechnology , genetics , biochemistry , amino acid , gene
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.