Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms.

Elkins, Jonathan M; Gileadi, Carina; Shrestha, Leela; Phillips, Claire; Wang, Jing; Muniz, João R C; Doyle, Declan A

Abstract:

PDZ domains most commonly bind the C-terminus of their protein targets. Typically the C-terminal four residues of the protein target are considered as the binding motif, particularly the C-terminal residue (P0) and third-last residue (P-2) that form the major contacts with the PDZ domain's "binding groove". We solved crystal structures of seven human PDZ domains, including five of the seven PDLIM family members. The structures of GRASP, PDLIM2, PDLIM5, and PDLIM7 show a binding mode with only...

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APA Style

Elkins, J. M., Gileadi, C., Shrestha, L., Phillips, C., Wang, J., Muniz, J. R. C., & Doyle, D. A. (2010). Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms. Protein Science : a Publication of the Protein Society, 19(4), 731–741.

MLA Style

Elkins, Jonathan M., et al. “Unusual Binding Interactions in PDZ Domain Crystal Structures Help Explain Binding Mechanisms.” Protein Science : a Publication of the Protein Society, vol. 19, no. 4, 2010, pp. 731–41.

Chicago Style

Elkins, Jonathan M, Carina Gileadi, Leela Shrestha, Claire Phillips, Jing Wang, João R C Muniz, and Declan A Doyle. 2010. “Unusual Binding Interactions in PDZ Domain Crystal Structures Help Explain Binding Mechanisms.” Protein Science : a Publication of the Protein Society 19 (4): 731–41.
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