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In molecular biology, the cache domain is an extracellular protein domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2+ channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source.[1] The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.[2]
References
- ↑ "Cache - a signaling domain common to animal Ca(2+)-channel subunits and a class of prokaryotic chemotaxis receptors". Trends Biochem. Sci. 25 (11): 535–7. November 2000. doi:10.1016/s0968-0004(00)01672-8. PMID 11084361.
- ↑ "Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains". J. Mol. Biol. 307 (5): 1271–92. April 2001. doi:10.1006/jmbi.2001.4508. PMID 11292341.
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