Characterization of diverse internal binding specificities of PDZ domains by yeast two-hybrid screening of a special peptide library.
Protein-protein interactions (PPIs) are essential events to play important roles in a series of biological processes. There are probably more ways of PPIs than we currently realized. Structural and functional investigations of weak PPIs have lagged behind those of strong PPIs due to technical diffic...
Main Authors: | Yi Mu, Pengfei Cai, Siqi Hu, Sucan Ma, Youhe Gao |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3913781?pdf=render |
Similar Items
-
Novel nonphosphorylated peptides with conserved sequences selectively bind to Grb7 SH2 domain with affinity comparable to its phosphorylated ligand.
by: Dan Zhang, et al.
Published: (2012-01-01) -
Peptide binding properties of the three PDZ domains of Bazooka (Drosophila Par-3).
by: Cao Guo Yu, et al.
Published: (2014-01-01) -
Membrane Binding and Modulation of the PDZ Domain of PICK1
by: Simon Erlendsson, et al.
Published: (2015-10-01) -
PDZ domains and their binding partners: structure, specificity, and modification
by: Zheng Jie J, et al.
Published: (2010-05-01) -
Genome-wide analysis of PDZ domain binding reveals inherent functional overlap within the PDZ interaction network
by: Te Velthuis, A, et al.
Published: (2011)