1u38
From Proteopedia
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Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains
Overview
Members of the X11/Mint family of multidomain adaptor proteins are, composed of a divergent N terminus, a conserved PTB domain and a pair of, C-terminal PDZ domains. Many proteins can interact with the PDZ tandem of, X11 proteins, although the mechanism of such interactions is unclear. Here, we show that the highly conserved C-terminal tail of X11alpha folds back, and inserts into the target-binding groove of the first PDZ domain. The, binding of this tail occludes the binding of other target peptides. This, autoinhibited conformation of X11 requires that the two PDZ domains and, the entire C-terminal tail be covalently connected to form an integral, structural unit. The autoinhibited conformation of the X11 PDZ tandem, provides a mechanistic explanation for the unique target-binding, properties of the protein and hints at potential regulatory mechanisms for, the X11-target interactions.
About this Structure
1U38 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem., Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M, Nat Struct Mol Biol. 2005 Aug;12(8):722-8. Epub 2005 Jul 10. PMID:16007100
Page seeded by OCA on Mon Nov 12 19:30:59 2007
Categories: Homo sapiens | Protein complex | Chan, L.N. | Feng, W. | Fu, A. | He, C. | Ip, N.Y. | Long, J.F. | Xia, J. | Zhang, M. | Pdz domain | Protein trafficking | Scaffold protein | X11s/mints
