Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/96439
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dc.contributor.authorChua, Geok-Linen
dc.contributor.authorPatra, Alok Tanalaen
dc.contributor.authorTan, Suet Mienen
dc.contributor.authorBhattacharjya, Surajiten
dc.date.accessioned2013-05-07T06:13:21Zen
dc.date.accessioned2019-12-06T19:30:51Z-
dc.date.available2013-05-07T06:13:21Zen
dc.date.available2019-12-06T19:30:51Z-
dc.date.copyright2013en
dc.date.issued2013en
dc.identifier.citationChua, 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).en
dc.identifier.issn1932-6203en
dc.identifier.urihttps://hdl.handle.net/10356/96439-
dc.description.abstractIntegrins 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.en
dc.language.isoenen
dc.relation.ispartofseriesPLoS ONEen
dc.rights© 2013 The Author(s).en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleNMR structure of integrin α4 cytosolic tail and Its interactions with paxillinen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1371/journal.pone.0055184en
dc.description.versionPublished versionen
dc.identifier.pmid23383101-
item.fulltextWith Fulltext-
item.grantfulltextopen-
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