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

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 monomycol...

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Publication status:
Published

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Publisher copy:
10.4049/jimmunol.172.4.2382

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Journal:
Journal of immunology (Baltimore, Md. : 1950)
Volume:
172
Issue:
4
Pages:
2382-2388
Publication date:
2004-02-05
DOI:
EISSN:
1550-6606
ISSN:
0022-1767
URN:
uuid:4ccbb570-5c97-4286-a302-89c84db9b776
Source identifiers:
15762
Local pid:
pubs:15762

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