Target sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin.
AUTOR(ES)
Houdusse, A
RESUMO
Some of the rules for how members of the calmodulin (CaM) superfamily bind to target peptides are revealed by the crystal structure of the regulatory domain of scallop myosin. The structure shows that the IQ motif of the heavy chain in this invertebrate myosin imposes constraints on both the positioning and conformation of the individual lobes of the light chains. In contrast, analysis of the contact residues in the targets bound by Ca(2+)-CaM reveals how the structure of CaM accommodates a broader range of sequences consonant with this protein's functional diversity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=40668Documentos Relacionados
- Isolation of the regulatory domain of scallop myosin: role of the essential light chain in calcium binding.
- Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin.
- Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase.
- Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue.
- Structure of the light chain-binding domain of myosin V
