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Domain binding and function: The calponin homology (CH) domain is a protein module of approximately 110 amino acids present in cytoskeletal and signal transduction proteins. Two CH domains in tandem form an F-actin binding region at the N-termini of spectrin-like proteins such as dystrophin and alpha-actinin. Such tandem CH domains bind F-actin with 5 - 50 µM affinity and cross-link actin filaments into bundles and networks. CH domains can be subdivided into at least three types. Type 1 and 2 are found together in tandem in cytoskeletal proteins such as dystrophin, spectrin and filamin. Type 3 CH domains are found in proteins that regulate muscle contraction, such as calponin, as well as in signaling proteins such as Vav, ARHGEF6 and IQGAP. Type 3 CH domains may not interact directly with actin, but rather act as regulatory domains or protein-protein interaction scaffolds to modulate the activity of proteins in which they are present. Structure Reference: Banuelos, S. et al. (1998) Structure 6(11), 1419-1431.
Examples of Domain Proteins:
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Binding Examples:
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CH domain proteins |  |
Binding partners |  |
| beta-spectrin | F-actin | |||
| Fimbrin | F-actin | |||
| Dystrophin | F-actin |
