- 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...
Expand abstract - Publication status:
- Published
- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2004
Journal article
The crystal structure of human CD1b with a bound bacterial glycolipid.
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