Bulletin of the American Physical Society
APS March Meeting 2011
Volume 56, Number 1
Monday–Friday, March 21–25, 2011; Dallas, Texas
Abstract: S1.00126 : InaD PDZs 4-5 Act as an Allosterically-Regulated Dynamic Scaffold
Author:
The Drosophila scaffolding protein InaD is required for proper visual
signaling. We previously identified that the fifth PDZ domain of InaD
undergoes light-dependent PKC-mediated formation of a disulfide bond which
disrupts the binding site. We investigated the interaction of this switch
with the adjacent PDZ4 of InaD. We showed that PDZ4 destabilizes the
disulfide bond and promotes binding of PDZ5 to its ligand, indicating a
previously unidentified allosteric interaction between the two domains. We
solved the structure of PDZ45 to 2.4{\AA}, which revealed that PDZ4 forms an
extensive interface with PDZ5 but does not alter its conformation. NMR HSQC
spectra, however, indicated that nearly all of PDZ5 is in a different
chemical environment in PDZ45. Finally, we identified that PDZ45 is
phosphorylated by PKC in vitro at a site located near the domain interface.
Intriguingly, the disulfide bond in PDZ5 is an evolutionary adaptation of
just fast-flying flies, revealing the remarkable ability of evolution to
rapidly build novel regulatory features into scaffolding proteins.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2011.MAR.S1.126
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