Structural highlights
Publication Abstract from PubMed
The enzyme phospholipase C-beta (PLCbeta) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the G(q) family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCbeta (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCbeta3 considerably increase basal activity and diminish stimulation by Galpha(q). Galpha(q) binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCbeta.
An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galpha(q) activation.,Lyon AM, Tesmer VM, Dhamsania VD, Thal DM, Gutierrez J, Chowdhury S, Suddala KC, Northup JK, Tesmer JJ Nat Struct Mol Biol. 2011 Aug 7;18(9):999-1005. doi: 10.1038/nsmb.2095. PMID:21822282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lyon AM, Tesmer VM, Dhamsania VD, Thal DM, Gutierrez J, Chowdhury S, Suddala KC, Northup JK, Tesmer JJ. An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galpha(q) activation. Nat Struct Mol Biol. 2011 Aug 7;18(9):999-1005. doi: 10.1038/nsmb.2095. PMID:21822282 doi:10.1038/nsmb.2095
