1uqs

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1uqs, resolution 3.10Å

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THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID

Overview

The human MHC class I-like molecule CD1b is distinctive among CD1 alleles, in that it is capable of presenting a set of glycolipid species that show, a very broad range of variation in the lengths of their acyl chains. A, structure of CD1b complexed with relatively short acyl chain glycolipids, plus detergent suggested how an interlinked network of channels within the, Ag-binding groove could accommodate acyl chain lengths of up to 80, carbons. The structure of CD1b complexed with glucose monomycolate, reported in this study, confirms this hypothesis and illustrates how the, distinctive substituents of intracellular bacterial glycolipids can be, accommodated. The Ag-binding groove of CD1b is, uniquely among CD1, alleles, partitioned into channels suitable for the compact accommodation, of ... [(full description)]

About this Structure

1UQS is a [Protein complex] structure of sequences from [Homo sapiens] with GMM as [ligand]. Full crystallographic information is available from [OCA].

Reference

The crystal structure of human CD1b with a bound bacterial glycolipid., Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY, J Immunol. 2004 Feb 15;172(4):2382-8. PMID:14764708

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