5l2k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5l2k is ON HOLD until Paper Publication
+
==Crystal structure of GEM42 TCR-CD1b-GMM complex==
 +
<StructureSection load='5l2k' size='340' side='right' caption='[[5l2k]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5l2k]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L2K FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6UL:TETRACOSYL+PALMITATE'>6UL</scene>, <scene name='pdbligand=70E:6-O-[(2R,3R)-3-HYDROXY-2-TETRADECYLDOCOSANOYL]-ALPHA-L-IDOPYRANOSE'>70E</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5l2j|5l2j]]</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=5l2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2k OCA], [http://pdbe.org/5l2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l2k RCSB], [http://www.ebi.ac.uk/pdbsum/5l2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2k 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/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> [[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.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
CD1 proteins present microbial lipids to T cells. Germline-encoded mycolyl lipid-reactive (GEM) T cells with conserved alphabeta T cell receptors (TCRs) recognize CD1b presenting mycobacterial mycolates. As the molecular basis underpinning TCR recognition of CD1b remains unknown, here we determine the structure of a GEM TCR bound to CD1b presenting glucose-6-O-monomycolate (GMM). The GEM TCR docks centrally above CD1b, whereby the conserved TCR alpha-chain extensively contacts CD1b and GMM. Through mutagenesis and study of T cells from tuberculosis patients, we identify a consensus CD1b footprint of TCRs present among GEM T cells. Using both the TCR alpha- and beta-chains as tweezers to surround and grip the glucose moiety of GMM, GEM TCRs create a highly specific mechanism for recognizing this mycobacterial glycolipid.
-
Authors:
+
T cell receptor recognition of CD1b presenting a mycobacterial glycolipid.,Gras S, Van Rhijn I, Shahine A, Cheng TY, Bhati M, Tan LL, Halim H, Tuttle KD, Gapin L, Le Nours J, Moody DB, Rossjohn J Nat Commun. 2016 Oct 27;7:13257. doi: 10.1038/ncomms13257. PMID:27807341<ref>PMID:27807341</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5l2k" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Gras, S]]
 +
[[Category: Nours, J Le]]
 +
[[Category: Rossjohn, J]]
 +
[[Category: Shahine, A]]
 +
[[Category: Cd1b]]
 +
[[Category: Gem t cell]]
 +
[[Category: Gem42]]
 +
[[Category: Gmm]]
 +
[[Category: Immune system]]
 +
[[Category: Lipid]]
 +
[[Category: Mtb]]
 +
[[Category: T cell]]
 +
[[Category: Tb]]
 +
[[Category: Tcr]]
 +
[[Category: Tuberculosis]]

Revision as of 19:39, 9 December 2016

Crystal structure of GEM42 TCR-CD1b-GMM complex

5l2k, resolution 3.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools