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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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C2 domain conformational changes in phospholipase C-delta 1.

The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 A and creating a gap large enough to bind a phospholipid headgroup.[1]

References

  1. C2 domain conformational changes in phospholipase C-delta 1. Grobler, J.A., Essen, L.O., Williams, R.L., Hurley, J.H. Nat. Struct. Biol. (1996) [Pubmed]
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