6j2h

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Current revision (10:18, 4 December 2019) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6j2h is ON HOLD until Paper Publication
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==Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 mutant (Met52 Asp53 Leu54 deleted) in complex with Hendra virus-derived peptide HeV1==
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<StructureSection load='6j2h' size='340' side='right'caption='[[6j2h]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6j2h]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_flying_fox Black flying fox] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J2H FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ptal-N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9402 Black flying fox]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=6j2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2h OCA], [http://pdbe.org/6j2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j2h RCSB], [http://www.ebi.ac.uk/pdbsum/6j2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2h ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[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>
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== Function ==
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[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans.
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Authors:
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Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.,Lu D, Liu K, Zhang D, Yue C, Lu Q, Cheng H, Wang L, Chai Y, Qi J, Wang LF, Gao GF, Liu WJ PLoS Biol. 2019 Sep 9;17(9):e3000436. doi: 10.1371/journal.pbio.3000436., eCollection 2019 Sep. PMID:31498797<ref>PMID:31498797</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6j2h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Black flying fox]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Chai, Y]]
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[[Category: Cheng, H]]
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[[Category: Gao, G F]]
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[[Category: Liu, K F]]
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[[Category: Liu, W J]]
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[[Category: Lu, D]]
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[[Category: Lu, Q]]
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[[Category: Qi, J X]]
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[[Category: Yue, C]]
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[[Category: Immune system]]

Current revision

Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 mutant (Met52 Asp53 Leu54 deleted) in complex with Hendra virus-derived peptide HeV1

PDB ID 6j2h

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