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The crystal structure of human CD1b with a bound bacterial glycolipid

The crystal structure of human CD1b with a bound bacterial glycolipid
The crystal structure of human CD1b with a bound bacterial glycolipid
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.

0022-1767
2382-2388
Batuwangala, Thil
c097f8c8-a20f-4ad0-9754-4432980ee348
Shepherd, Dawn
b34728f7-7f4e-4f73-b5f3-79b495d06c92
Gadola, Stephan D.
ef2fa6cf-2ccc-4fea-a7a5-cc03a9d13ab1
Gibson, Kevin J.
44e45cfe-d42d-49fd-851c-3f7194f2581e
Zaccai, Nathan R.
5e5781cf-1bb8-4a2f-b72d-dd89139fe3cd
Fersht, Alan R.
b5145a83-e9cb-426f-8722-f60eb9aa59a5
Besra, Gurdyal
a6dd0a79-8461-41fd-9e3f-9a1399dd2d1c
Cerundolo, Vincenzo
813bcd4a-ca19-48a3-86e4-71d131e2065a
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Batuwangala, Thil
c097f8c8-a20f-4ad0-9754-4432980ee348
Shepherd, Dawn
b34728f7-7f4e-4f73-b5f3-79b495d06c92
Gadola, Stephan D.
ef2fa6cf-2ccc-4fea-a7a5-cc03a9d13ab1
Gibson, Kevin J.
44e45cfe-d42d-49fd-851c-3f7194f2581e
Zaccai, Nathan R.
5e5781cf-1bb8-4a2f-b72d-dd89139fe3cd
Fersht, Alan R.
b5145a83-e9cb-426f-8722-f60eb9aa59a5
Besra, Gurdyal
a6dd0a79-8461-41fd-9e3f-9a1399dd2d1c
Cerundolo, Vincenzo
813bcd4a-ca19-48a3-86e4-71d131e2065a
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be

Batuwangala, Thil, Shepherd, Dawn, Gadola, Stephan D., Gibson, Kevin J., Zaccai, Nathan R., Fersht, Alan R., Besra, Gurdyal, Cerundolo, Vincenzo and Jones, E. Yvonne (2004) The crystal structure of human CD1b with a bound bacterial glycolipid. The Journal of Immunology, 172 (4), 2382-2388. (PMID:14764708)

Record type: Article

Abstract

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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More information

Published date: 15 February 2004

Identifiers

Local EPrints ID: 175465
URI: http://eprints.soton.ac.uk/id/eprint/175465
ISSN: 0022-1767
PURE UUID: 0c75706b-ce7d-473a-9b2a-48e64c0753b7

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Date deposited: 23 Feb 2011 15:41
Last modified: 16 Jul 2019 23:46

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Contributors

Author: Thil Batuwangala
Author: Dawn Shepherd
Author: Stephan D. Gadola
Author: Kevin J. Gibson
Author: Nathan R. Zaccai
Author: Alan R. Fersht
Author: Gurdyal Besra
Author: Vincenzo Cerundolo
Author: E. Yvonne Jones

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