1uqs

From Proteopedia

(Difference between revisions)

Revision as of 07:47, 28 March 2018

The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid

Structural highlights

1uqs is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1gzp, 1gzq, 1a1m, 1a1n, 1a1o, 1a6z, 1a9b, 1a9e, 1agb, 1agc, 1agd, 1age, 1agf, 1akj, 1ao7, 1b0g, 1ce6, 1de4, 1e27, 1e28, 1eey, 1eez, 1efx, 1exu, 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
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY. The crystal structure of human CD1b with a bound bacterial glycolipid. J Immunol. 2004 Feb 15;172(4):2382-8. PMID:14764708

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uqs"

@@ Line 1: / Line 1: @@
-==THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID==
+==The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid==
 <StructureSection load='1uqs' size='340' side='right' caption='[[1uqs]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GMM:GLUCOSE+MONOMYCOLATE'>GMM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gzp|1gzp]], [[1gzq|1gzq]], [[1a1m|1a1m]], [[1a1n|1a1n]], [[1a1o|1a1o]], [[1a6z|1a6z]], [[1a9b|1a9b]], [[1a9e|1a9e]], [[1agb|1agb]], [[1agc|1agc]], [[1agd|1agd]], [[1age|1age]], [[1agf|1agf]], [[1akj|1akj]], [[1ao7|1ao7]], [[1b0g|1b0g]], [[1ce6|1ce6]], [[1de4|1de4]], [[1e27|1e27]], [[1e28|1e28]], [[1eey|1eey]], [[1eez|1eez]], [[1efx|1efx]], [[1exu|1exu]], [[1hhg|1hhg]], [[1hhh|1hhh]], [[1hhi|1hhi]], [[1hhj|1hhj]], [[1hhk|1hhk]], [[1hla|1hla]], [[1hsa|1hsa]], [[1hsb|1hsb]], [[1i4f|1i4f]], [[1i7r|1i7r]], [[1i7t|1i7t]], [[1i7u|1i7u]], [[1im3|1im3]], [[1im9|1im9]], [[1jf1|1jf1]], [[1jgd|1jgd]], [[1jge|1jge]], [[1jht|1jht]], [[1jnj|1jnj]], [[1k5n|1k5n]], [[1kpr|1kpr]], [[1ktl|1ktl]], [[1lds|1lds]], [[1m05|1m05]], [[1m6o|1m6o]], [[1mi5|1mi5]], [[1of2|1of2]], [[1oga|1oga]], [[1ogt|1ogt]], [[1qlf|1qlf]], [[1qqd|1qqd]], [[1tmc|1tmc]], [[2clr|2clr]], [[2hla|2hla]], [[3hla|3hla]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqs OCA], [http://pdbe.org/1uqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uqs RCSB], [http://www.ebi.ac.uk/pdbsum/1uqs PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqs OCA], [http://pdbe.org/1uqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uqs RCSB], [http://www.ebi.ac.uk/pdbsum/1uqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqs ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>   Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
-== Function ==
-[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uq/1uqs_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uq/1uqs_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1uqs

From Proteopedia

Revision as of 07:47, 28 March 2018

The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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