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lüll CH domains revisited Stradal T; Kranewitter W; Winder SJ; Gimona MFEBS Lett 1998[Jul]; 431 (2): 134-7A sequence motif of about 100 amino acids, termed the 'calponin homology domain' has been suggested to confer actin binding to a variety of cytoskeletal and signalling molecules. Here we analyse and compare the sequences of all calponin homology domain-containing proteins identified to date. We propose that single calponin homology domains do not confer actin-binding per se and that the actin-binding motifs of cross-linking proteins, which comprise two disparate calponin homology domains, represent a unique protein module.|Actins/*metabolism[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Calcium-Binding Proteins/*chemistry/metabolism[MESH]|Calponins[MESH]|Databases, Factual[MESH]|Humans[MESH]|Microfilament Proteins[MESH]|Molecular Sequence Data[MESH]|Phylogeny[MESH]|Protein Conformation[MESH]|Sequence Homology, Amino Acid[MESH] |