1uqs
From Proteopedia
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==Overview== | ==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 lengthy acyl chains. The current crystal structure illustrates for the, first time the binding of a natural bacterial lipid Ag to CD1b and shows, how its novel structural features fit this molecule for its role in the, immune response to intracellular bacteria. | 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 lengthy acyl chains. The current crystal structure illustrates for the, first time the binding of a natural bacterial lipid Ag to CD1b and shows, how its novel structural features fit this molecule for its role in the, immune response to intracellular bacteria. | ||
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: mhc]] | [[Category: mhc]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:37:40 2007'' |
Revision as of 17:31, 12 November 2007
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THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID
Contents |
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 lengthy acyl chains. The current crystal structure illustrates for the, first time the binding of a natural bacterial lipid Ag to CD1b and shows, how its novel structural features fit this molecule for its role in the, immune response to intracellular bacteria.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1UQS is a Protein complex structure of sequences from Homo sapiens with GMM as ligand. Structure known Active Site: AC1. 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
Page seeded by OCA on Mon Nov 12 19:37:40 2007
Categories: Homo sapiens | Protein complex | Batuwangala, T. | Besra, G.S. | Cerundolo, V. | Gadola, S.D. | Gibson, K.J.C. | Jones, E.Y. | Shepherd, D. | Zaccai, N.R. | GMM | Antigen presentation | Cd1b | Gmm | Lipid | Mhc
