1U39

Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains

Summary for 1U39

• Entry DOI: 10.2210/pdb1u39/pdb
• Related: 1U37 1U38 1U3B
• Descriptor: amyloid beta A4 precursor protein-binding, family A, member 1 (1 entity in total)
• Functional Keywords: x11s/mints, pdz domain, scaffold protein, protein trafficking, protein transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8720.25

Authors

Feng, W.,Long, J.-F.,Chan, L.-N.,He, C.,Fu, A.,Xia, J.,Ip, N.Y.,Zhang, M. (deposition date: 2004-07-21, release date: 2005-07-26, Last modification date: 2024-05-29)

Primary citation

Long, J.-F.,Feng, W.,Wang, R.,Chan, L.-N.,Ip, F.C.,Xia, J.,Ip, N.Y.,Zhang, M.
Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem
Nat.Struct.Mol.Biol., 12:722-728, 2005

PubMed Abstract: 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.

PubMed: 16007100
DOI: 10.1038/nsmb958

Experimental method

SOLUTION NMR