An Exquisitely Specific PDZ/Target Recognition Revealed by the Structure of INAD PDZ3 in Complex with TRP Channel Tail
Abstract
No abstract availableKeywords
Funding Information
- RGC of Hong Kong (663811, 663812, SEG_HKUST06, AoE-M09-12)
- Minister of Science and Technology of China (2014CB910201)
- National Natural Science Foundation of China (31400647)
- Guangdong Natural Science Foundation (S2012010008170)
This publication has 41 references indexed in Scilit:
- Overview of theCCP4 suite and current developmentsActa Crystallographica Section D Structural Biology, 2011
- Genome-Wide Analysis of PDZ Domain Binding Reveals Inherent Functional Overlap within the PDZ Interaction NetworkPLOS ONE, 2011
- Features and development of CootActa Crystallographica Section D Structural Biology, 2010
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D Structural Biology, 2010
- A Specificity Map for the PDZ Domain FamilyPLOS Biology, 2008
- Anchoring TRP to the INAD macromolecular complex requires the last 14 residues in its carboxyl terminusJournal of Neurochemistry, 2007
- PDZ Domain Binding Selectivity Is Optimized Across the Mouse ProteomeScience, 2007
- Phasercrystallographic softwareJournal of Applied Crystallography, 2007
- Internal recognition through PDZ domain plasticity in the Par-6–Pals1 complexNature Structural & Molecular Biology, 2004
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995