Cargando…
New Conformational State of NHERF1-CXCR2 Signaling Complex Captured by Crystal Lattice Trapping
NHERF1 is a PDZ adaptor protein that scaffolds the assembly of diverse signaling complexes and has been implicated in many cancers. However, little is known about the mechanism responsible for its scaffolding promiscuity or its ability to bind to multiple targets. Computational studies have indicate...
Autores principales: | Jiang, Yuanyuan, Lu, Guorong, Trescott, Laura R., Hou, Yuning, Guan, Xiaoqing, Wang, Shuo, Stamenkovich, Angelique, Brunzelle, Joseph, Sirinupong, Nualpun, Li, Chunying, Yang, Zhe |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3858284/ https://www.ncbi.nlm.nih.gov/pubmed/24339979 http://dx.doi.org/10.1371/journal.pone.0081904 |
Ejemplares similares
-
Structural Insights into Neutrophilic Migration Revealed by the Crystal Structure of the Chemokine Receptor CXCR2 in Complex with the First PDZ Domain of NHERF1
por: Lu, Guorong, et al.
Publicado: (2013) -
Crystal Structures of Histone and p53 Methyltransferase SmyD2 Reveal a Conformational Flexibility of the Autoinhibitory C-Terminal Domain
por: Jiang, Yuanyuan, et al.
Publicado: (2011) -
Structure and Function of SET and MYND Domain-Containing Proteins
por: Spellmon, Nicholas, et al.
Publicado: (2015) -
New open conformation of SMYD3 implicates conformational selection and allostery
por: Spellmon, Nicholas, et al.
Publicado: (2016) -
Molecular Dynamics Simulation Reveals Correlated Inter-Lobe Motion in Protein Lysine Methyltransferase SMYD2
por: Spellmon, Nicholas, et al.
Publicado: (2015)