1gzq: Difference between revisions
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<StructureSection load='1gzq' size='340' side='right'caption='[[1gzq]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='1gzq' size='340' side='right'caption='[[1gzq]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gzq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1gzq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GZQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PII:2-[(HYDROXY{[(2R,3R,5S,6R)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL)OXY]-1-[(PALMITOYLOXY)METHYL]ETHYL+HEPTADECANOATE'>PII</scene>, <scene name='pdbligand=TWT:DOCOSANE'>TWT</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PII:2-[(HYDROXY{[(2R,3R,5S,6R)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL)OXY]-1-[(PALMITOYLOXY)METHYL]ETHYL+HEPTADECANOATE'>PII</scene>, <scene name='pdbligand=TWT:DOCOSANE'>TWT</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzq OCA], [https://pdbe.org/1gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gzq RCSB], [https://www.ebi.ac.uk/pdbsum/1gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gzq ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzq OCA], [https://pdbe.org/1gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gzq RCSB], [https://www.ebi.ac.uk/pdbsum/1gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gzq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CD1B_HUMAN CD1B_HUMAN] Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:10981968</ref> <ref>PMID:14716313</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/1gzq_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/1gzq_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 30: | Line 32: | ||
==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
*[[CD1|CD1]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cerundolo | [[Category: Cerundolo V]] | ||
[[Category: Gadola | [[Category: Gadola SD]] | ||
[[Category: Harlos | [[Category: Harlos K]] | ||
[[Category: Jones | [[Category: Jones EY]] | ||
[[Category: Ritter | [[Category: Ritter G]] | ||
[[Category: Schmidt | [[Category: Schmidt RR]] | ||
[[Category: Shepherd | [[Category: Shepherd D]] | ||
[[Category: Zaccai | [[Category: Zaccai NR]] | ||
Latest revision as of 11:29, 6 November 2024
CD1b in complex with PhophatidylinositolCD1b in complex with Phophatidylinositol
Structural highlights
FunctionCD1B_HUMAN Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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