1gzq: Difference between revisions
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==Overview== | ==Overview== | ||
The human genome encodes five nonpolymorphic major histocompatibility, complex class I-like glycoproteins, CD1a to CD1e, that present lipid, antigens for specific recognition by T lymphocytes. Using single alkyl, chain detergents, we developed a protocol to generate recombinant human, CD1b-lipid complexes. We present here the crystal structures of CD1b in, complex with either phosphatidylinositol or ganglioside GM2 at 2.3 A and, 2.8 A resolutions, respectively. The antigen-binding groove houses four, interlinked hydrophobic channels that are occupied by the alkyl chains of, the glycolipid plus two detergent molecules. A distinct exit beneath the, alpha 2 helix further contributes to the plasticity of the binding groove., These structures reveal the mechanism by which two alkyl chain lipids bind, to CD1b, and how CD1b can adapt to ligands of different alkyl chain, length. They also suggest how very long alkyl chains, such as those of, mycolic acid, could be fully contained within the binding groove. These, results extend the spectrum of potential CD1b ligands by revealing that, in addition to two alkyl chain lipids, mono-alkyl and triple-alkyl chain, lipids can be accommodated in the binding groove. | The human genome encodes five nonpolymorphic major histocompatibility, complex class I-like glycoproteins, CD1a to CD1e, that present lipid, antigens for specific recognition by T lymphocytes. Using single alkyl, chain detergents, we developed a protocol to generate recombinant human, CD1b-lipid complexes. We present here the crystal structures of CD1b in, complex with either phosphatidylinositol or ganglioside GM2 at 2.3 A and, 2.8 A resolutions, respectively. The antigen-binding groove houses four, interlinked hydrophobic channels that are occupied by the alkyl chains of, the glycolipid plus two detergent molecules. A distinct exit beneath the, alpha 2 helix further contributes to the plasticity of the binding groove., These structures reveal the mechanism by which two alkyl chain lipids bind, to CD1b, and how CD1b can adapt to ligands of different alkyl chain, length. They also suggest how very long alkyl chains, such as those of, mycolic acid, could be fully contained within the binding groove. These, results extend the spectrum of potential CD1b ligands by revealing that, in addition to two alkyl chain lipids, mono-alkyl and triple-alkyl chain, lipids can be accommodated in the binding groove. | ||
==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: phophatidylinositol]] | [[Category: phophatidylinositol]] | ||
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Revision as of 18:04, 12 November 2007
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CD1B IN COMPLEX WITH PHOPHATIDYLINOSITOL
OverviewOverview
The human genome encodes five nonpolymorphic major histocompatibility, complex class I-like glycoproteins, CD1a to CD1e, that present lipid, antigens for specific recognition by T lymphocytes. Using single alkyl, chain detergents, we developed a protocol to generate recombinant human, CD1b-lipid complexes. We present here the crystal structures of CD1b in, complex with either phosphatidylinositol or ganglioside GM2 at 2.3 A and, 2.8 A resolutions, respectively. The antigen-binding groove houses four, interlinked hydrophobic channels that are occupied by the alkyl chains of, the glycolipid plus two detergent molecules. A distinct exit beneath the, alpha 2 helix further contributes to the plasticity of the binding groove., These structures reveal the mechanism by which two alkyl chain lipids bind, to CD1b, and how CD1b can adapt to ligands of different alkyl chain, length. They also suggest how very long alkyl chains, such as those of, mycolic acid, could be fully contained within the binding groove. These, results extend the spectrum of potential CD1b ligands by revealing that, in addition to two alkyl chain lipids, mono-alkyl and triple-alkyl chain, lipids can be accommodated in the binding groove.
DiseaseDisease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this StructureAbout this Structure
1GZQ is a Protein complex structure of sequences from Homo sapiens with NO3, PII, D12 and TWT as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains., Gadola SD, Zaccai NR, Harlos K, Shepherd D, Castro-Palomino JC, Ritter G, Schmidt RR, Jones EY, Cerundolo V, Nat Immunol. 2002 Aug;3(8):721-6. Epub 2002 Jul 15. PMID:12118248
Page seeded by OCA on Mon Nov 12 17:10:36 2007