1uqs

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[[Image:1uqs.jpg|left|200px]]<br /><applet load="1uqs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uqs, resolution 3.10&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID'''<br />
 
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==Overview==
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==The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid==
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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.
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<StructureSection load='1uqs' size='340' side='right'caption='[[1uqs]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uqs]] 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=1UQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GMM:GLUCOSE+MONOMYCOLATE'>GMM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqs OCA], [https://pdbe.org/1uqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqs RCSB], [https://www.ebi.ac.uk/pdbsum/1uqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uq/1uqs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uqs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Disease==
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The crystal structure of human CD1b with a bound bacterial glycolipid.,Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY J Immunol. 2004 Feb 15;172(4):2382-8. PMID:14764708<ref>PMID:14764708</ref>
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Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1UQS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GMM:'>GMM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gmm+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQS OCA].
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</div>
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<div class="pdbe-citations 1uqs" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The crystal structure of human CD1b with a bound bacterial glycolipid., Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY, J Immunol. 2004 Feb 15;172(4):2382-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14764708 14764708]
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[CD1|CD1]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Batuwangala, T.]]
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[[Category: Batuwangala T]]
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[[Category: Besra, G.S.]]
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[[Category: Besra GS]]
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[[Category: Cerundolo, V.]]
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[[Category: Cerundolo V]]
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[[Category: Gadola, S.D.]]
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[[Category: Gadola SD]]
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[[Category: Gibson, K.J.C.]]
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[[Category: Gibson KJC]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones EY]]
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[[Category: Shepherd, D.]]
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[[Category: Shepherd D]]
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[[Category: Zaccai, N.R.]]
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[[Category: Zaccai NR]]
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[[Category: GMM]]
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[[Category: antigen presentation]]
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[[Category: cd1b]]
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[[Category: gmm]]
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[[Category: lipid]]
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[[Category: mhc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:03:52 2008''
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Current revision

The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid

PDB ID 1uqs

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