1UQS
The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid
Summary for 1UQS
| Entry DOI | 10.2210/pdb1uqs/pdb |
| Related | 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 1B0G 1CE6 1DE4 1E27 1E28 1EEY 1EEZ 1EFX 1EXU 1GZP 1GZQ 1HHG 1HHH 1HHI 1HHJ 1HHK 1HLA 1HSA 1HSB 1I4F 1I7R 1I7T 1I7U 1IM3 1IM9 1JF1 1JGD 1JGE 1JHT 1JNJ 1K5N 1KPR 1KTL 1LDS 1M05 1M6O 1MI5 1OF2 1OGA 1OGT 1QLF 1QQD 1TMC 2CLR 2HLA 3HLA |
| Descriptor | T-CELL SURFACE GLYCOPROTEIN CD1B, BETA-2-MICROGLOBULIN, GLUCOSE MONOMYCOLATE, ... (4 entities in total) |
| Functional Keywords | glycoprotein, lipid, gmm, cd1b, mhc, antigen presentation |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 2 |
| Total formula weight | 46015.27 |
| Authors | Batuwangala, T.,Shepherd, D.,Gadola, S.D.,Gibson, K.J.C.,Zaccai, N.R.,Besra, G.S.,Cerundolo, V.,Jones, E.Y. (deposition date: 2003-10-16, release date: 2003-10-30, Last modification date: 2024-11-20) |
| Primary citation | Batuwangala, T.,Shepherd, D.,Gadola, S.D.,Gibson, K.J.,Zaccai, N.R.,Fersht, A.R.,Besra, G.S.,Cerundolo, V.,Jones, E.Y. The crystal structure of human CD1b with a bound bacterial glycolipid. J Immunol., 172:2382-2388, 2004 Cited by PubMed 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. PubMed: 14764708DOI: 10.4049/jimmunol.172.4.2382 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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