Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/96439
Title: NMR structure of integrin α4 cytosolic tail and Its interactions with paxillin
Authors: Chua, Geok-Lin
Patra, Alok Tanala
Tan, Suet Mien
Bhattacharjya, Surajit
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2013
Source: Chua, G. L., Patra, A. T., Tan, S. M., & Bhattacharjya, S. (2013). NMR Structure of Integrin α4 Cytosolic Tail and Its Interactions with Paxillin. PLoS ONE, 8(1).
Series/Report no.: PLoS ONE
Abstract: Integrins are a group of transmembrane signaling proteins that are important in biological processes such as cell adhesion, proliferation and migration. Integrins are α/β hetero-dimers and there are 24 different integrins formed by specific combinations of 18 α and 8 β 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 α4 CT (Lys968-Asp999) and characterize its interactions with the adaptor protein paxillin. The α4 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. 15N-1H HSQC NMR experiments reveal interactions of the α4 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 α4 CT bindinginduced chemical shift changes. Furthermore, NMR studies using LD-containing peptides showed predominant interactions between LD3 and LD4 of paxillin and α4 CT. Docked structures of the α4 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 α CTs of integrins and interactions of integrin α4 CT with the adaptor protein paxillin.
URI: https://hdl.handle.net/10356/96439
http://hdl.handle.net/10220/9896
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0055184
Rights: © 2013 The Author(s).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
16. NMR Structure of Integrin a4 Cytosolic Tail and Its.pdf792.94 kBAdobe PDFThumbnail
View/Open

SCOPUSTM   
Citations

8
checked on Sep 1, 2020

WEB OF SCIENCETM
Citations

8
checked on Oct 19, 2020

Page view(s)

478
checked on Oct 24, 2020

Download(s)

223
checked on Oct 24, 2020

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.