3ov6: Difference between revisions
New page: '''Unreleased structure''' The entry 3ov6 is ON HOLD Authors: Scharf, L., Li, N.S., Hawk, A.J., Garzon, D., Zhang, T., Kazen, A.R., Shah, S., Haddadian, E.J., Saghatelian, A., Faraldo-G... |
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The | ==CD1c in complex with MPM (mannosyl-beta1-phosphomycoketide)== | ||
<StructureSection load='3ov6' size='340' side='right'caption='[[3ov6]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ov6]] is a 1 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=3OV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OV6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.502Å</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=MK0:1-O-[(S)-HYDROXY{[(4S,8S,16S,20S)-4,8,12,16,20-PENTAMETHYLHEPTACOSYL]OXY}PHOSPHORYL]-BETA-D-MANNOPYRANOSE'>MK0</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3ov6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ov6 OCA], [https://pdbe.org/3ov6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ov6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ov6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ov6 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://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 == | |||
[https://www.uniprot.org/uniprot/CD1C_HUMAN CD1C_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:10786796</ref> <ref>PMID:10890914</ref> <ref>PMID:10899914</ref> <ref>PMID:21167756</ref> [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> [https://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 molecules function to present lipid-based antigens to T cells. Here we present the crystal structure of CD1c at 2.5 A resolution, in complex with the pathogenic Mycobacterium tuberculosis antigen mannosyl-beta1-phosphomycoketide (MPM). CD1c accommodated MPM's methylated alkyl chain exclusively in the A' pocket, aided by a unique exit portal underneath the alpha1 helix. Most striking was an open F' pocket architecture lacking the closed cavity structure of other CD1 molecules, reminiscent of peptide binding grooves of classical major histocompatibility complex molecules. This feature, combined with tryptophan-fluorescence quenching during loading of a dodecameric lipopeptide antigen, provides a compelling model by which both the lipid and peptide moieties of the lipopeptide are involved in CD1c presentation of lipopeptides. | |||
The 2.5 a structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation.,Scharf L, Li NS, Hawk AJ, Garzon D, Zhang T, Fox LM, Kazen AR, Shah S, Haddadian EJ, Gumperz JE, Saghatelian A, Faraldo-Gomez JD, Meredith SC, Piccirilli JA, Adams EJ Immunity. 2010 Dec 14;33(6):853-62. PMID:21167756<ref>PMID:21167756</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ov6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[CD1|CD1]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams EJ]] | |||
[[Category: Faraldo-Gomez JD]] | |||
[[Category: Garzon D]] | |||
[[Category: Haddadian EJ]] | |||
[[Category: Hawk AJ]] | |||
[[Category: Kazen AR]] | |||
[[Category: Li NS]] | |||
[[Category: Meredith SC]] | |||
[[Category: Piccirilli JA]] | |||
[[Category: Saghatelian A]] | |||
[[Category: Scharf L]] | |||
[[Category: Shah S]] | |||
[[Category: Zhang T]] | |||