structure. Although the various CHD share relatively little amino acidsequence identity, a number of strictly conserved hydrophobic residuesgive rise to an almost unchanging hydrophobic core. Despite a commonoverall fold, different CHDs serve to interface with a wide variety of proteins involved in cytoskeleton dynamics and signal transduction.
CHDare classified into several families. The main calponin homology domainsare type-1 CHD, type-2 CHD and type-3 CHD. Caplonin homology domaintype-1 and type 2 are normally arranged in tandem and are found in manyactin-binding proteins. The type-2 CH domain can also exist as an isolatedCH-domain, and is found in a few proteins, including smoothelins.
Type-3CHD is found in several proteins including IQGAP and calponin and is asingle CH domain.Within this review the structure of CHDs and its interactions withcalcium will be discussed. These interactions with calcium and calmodulinare essential for cellular communication. Calcium acts as a ubiquitousintracellular messenger responsible for controlling numerous cellularresponses. A momentary rise in intracellular calcium concentrationinduces a conformational change in calmodulin, allowing it to bind tospecific domains on target proteins, predominately amphiphilic
The physiological effects of calponin homology domains with F-actin,Vav1, a guanine nucleotide exchange factor, smoothelin-like proteins andmicrotubules will also be introduced. The aim is to conclude whether theinteractions with the domains and proteins are dependent on calcium forcytoskeleton dynamics and signal transduction.
2. Structure of Calponin Homology Domains
The architecture of the CHD is dominated by four
-helices are comprised of 11-18 residues and are connected by long loops. There are also three short and less regular helices, which are minorsecondary structural elements. The structure can be described in terms of three layers, the core being composed of two parallel
-helices which are2