Related ArticlesNMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
PLoS One. 2013;8(1):e55184
Authors: Chua GL, Patra AT, Tan SM, Bhattacharjya S
Abstract
BACKGROUND: Integrins are a group of transmembrane signaling proteins that are important in biological processes such as cell adhesion, proliferation and migration. Integrins are ?/? hetero-dimers and there are 24 different integrins formed by specific combinations of 18 ? and 8 ? subunits in humans. Generally, each of these subunits has a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). CTs of integrins are important in bidirectional signal transduction and they associate with a large number of intracellular proteins.
PRINCIPAL FINDINGS: Using NMR spectroscopy, we determined the 3-D structure of the full-length ?4 CT (Lys968-Asp999) and characterize its interactions with the adaptor protein paxillin. The ?4 CT assumes an overall helical structure with a kink in its membrane proximal region. Residues Gln981-Asn997 formed a continuous helical conformation that may be sustained by potential ionic and/or hydrogen bond interactions and packing of aromatic-aliphatic side-chains. (15)N-(1)H HSQC NMR experiments reveal interactions of the ?4 CT C-terminal region with a fragment of paxillin (residues G139-K277) that encompassed LD2-LD4 repeats. Residues of these LD repeats including their adjoining linkers showed ?4 CT binding-induced chemical shift changes. Furthermore, NMR studies using LD-containing peptides showed predominant interactions between LD3 and LD4 of paxillin and ?4 CT. Docked structures of the ?4 CT with these LD repeats suggest possible polar and/or salt-bridge and non-polar packing interactions.
SIGNIFICANCE: The current study provides molecular insights into the structural diversity of ? CTs of integrins and interactions of integrin ?4 CT with the adaptor protein paxillin.
Ordered PhosphorylationEvents in Two IndependentCascades of the PTEN C-tail Revealed by NMR
Ordered PhosphorylationEvents in Two IndependentCascades of the PTEN C-tail Revealed by NMR
Florence Cordier, Alain Chaffotte, Elouan Terrien, Christophe Pre?haud, Franc?ois-Xavier Theillet, Muriel Delepierre, Monique Lafon, Henri Buc and Nicolas Wolff
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja310214g/aop/images/medium/ja-2012-10214g_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja310214g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/CgOsmhhExM8
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NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
Linear Mode
