UNSPECIFIED (2002) A structure for the trimeric MHC class II-associated invariant chain transmembrane domain. Journal of Molecular Biology, 320 (5). pp. 1109-1117. ISSN 0022-2836

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Abstract

The major histocompatibility complex (MHC)-associated invariant chain (Ii) contains a single transmembrane domain that forms trimers. Ii is involved in the assembly of the MHC and antigen presentation, and is thus central to the function of the immune system. Here, we show by attenuated total reflectance, Fourier transform infrared (ATR-FTIR) spectroscopy that the transmembrane domain is a-helical and we provide a structural model of the transmembrane domain obtained by a combination of site-specific infrared dichroism and molecular dynamics (MD) simulations. This work resolves the backbone structure of a transmembrane peptide by multiple C-13=O-18 labelling at ten different residues. A second purely computational approach, based on MD simulations of Ii transmembrane homologous sequences, yields a similar structure that is consistent with our experimental results. The structure presented forms a left-handed coiled coil with an average helix tilt of 13(+/-6)degrees; the residue Gln47 implicated in trimer formation forms strong interhelical contacts, Thr50 points to the inside of the trimeric coil and forms a network of hydrogen bonds. (C) 2002 Elsevier Science Ltd. All rights reserved.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	Journal of Molecular Biology
Publisher:	ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
ISSN:	0022-2836
Date:	26 July 2002
Volume:	320
Number:	5
Number of Pages:	9
Page Range:	pp. 1109-1117
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/10675

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