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Title: Structure and binding interface of the cytosolic tails of αXβ2 integrin
Authors: Chua, Geok-Lin
Tang, Xiao-Yan
Patra, Alok Tanala
Tan, Suet Mien
Bhattacharjya, Surajit
Issue Date: 2012
Source: Chua, G.-L., Tang, X.-Y., Patra, A. T., Tan, S.-M., & Bhattacharjya, S. (2012). Structure and binding interface of the cytosolic tails of αXβ2 integrin. PLoS ONE, 7(7).
Series/Report no.: PLoS ONE
Abstract: Integrins are signal transducer proteins involved in a number of vital physiological processes including cell adhesion, proliferation and migration. Integrin molecules are hetero-dimers composed of two distinct subunits, α and β. In humans, 18 α and 8 β subunits are combined into 24 different integrin molecules. Each of the subunit comprises a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). The CTs of integrins are vital for bidirectional signal transduction and in maintaining the resting state of the receptors. A large number of intracellular proteins have been found to interact with the CTs of integrins linking integrins to the cytoskeleton. Methodology/Principal Findings: In this work, we have investigated structure and interactions of CTs of the leukocyte specific integrin αXβ2. We determined the atomic resolution structure of a myristoylated CT of αX in perdeuterated dodecylphosphocholine (DPC) by NMR spectroscopy. Our results reveal that the 35-residue long CT of αX adopts an α-helical conformation for residues F4-N17 at the N-terminal region. The remaining residues located at the C-terminal segment of αX delineate a long loop of irregular conformations. A segment of the loop maintains packing interactions with the helical structure by an extended non-polar surface of the αX CT. Interactions between αX and β2 CTs are demonstrated by 15N-1H HSQC NMR experiments. We find that residues constituting the polar face of the helical conformation of αX are involved in interactions with the N-terminal residues of β2 CT. A docked structure of the CT complex indicates that a network of polar and/or salt-bridge interactions may sustain the heteromeric interactions.
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0041924
Schools: School of Biological Sciences 
Rights: © 2012 The Authors.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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