6v2o: Difference between revisions

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<StructureSection load='6v2o' size='340' side='right'caption='[[6v2o]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
<StructureSection load='6v2o' size='340' side='right'caption='[[6v2o]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6v2o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V2O FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V2O 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]] 1.27&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=6v2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v2o OCA], [https://pdbe.org/6v2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v2o RCSB], [https://www.ebi.ac.uk/pdbsum/6v2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v2o ProSAT]</span></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=6v2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v2o OCA], [https://pdbe.org/6v2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v2o RCSB], [https://www.ebi.ac.uk/pdbsum/6v2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v2o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U6BR87_HUMAN U6BR87_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Micropolymorphisms within human leukocyte antigen (HLA) class I molecules can change the architecture of the peptide-binding cleft, leading to differences in peptide presentation and T cell recognition. The impact of such HLA variation on natural killer (NK) cell recognition remains unclear. Given the differential association of HLA-B*57:01 and HLA-B*57:03 with the control of HIV, recognition of these HLA-B57 allomorphs by the killer cell immunoglobulin-like receptor (KIR) 3DL1 was compared. Despite differing by only two polymorphic residues, both buried within the peptide-binding cleft, HLA-B*57:01 more potently inhibited NK cell activation. Direct-binding studies showed KIR3DL1 to preferentially recognize HLA-B*57:01, particularly when presenting peptides with positively charged position (P)Omega-2 residues. In HLA-B*57:01, charged POmega-2 residues were oriented toward the peptide-binding cleft and away from KIR3DL1. In HLA-B*57:03, the charged POmega-2 residues protruded out from the cleft and directly impacted KIR3DL1 engagement. Accordingly, KIR3DL1 recognition of HLA class I ligands is modulated by both the peptide sequence and conformation, as determined by the HLA polymorphic framework, providing a rationale for understanding differences in clinical associations.
The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function.,Saunders PM, MacLachlan BJ, Pymm P, Illing PT, Deng Y, Wong SC, Oates CVL, Purcell AW, Rossjohn J, Vivian JP, Brooks AG Proc Natl Acad Sci U S A. 2020 May 13. pii: 1920570117. doi:, 10.1073/pnas.1920570117. PMID:32404419<ref>PMID:32404419</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6v2o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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*[[MHC 3D structures|MHC 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Maclachlan B]]
[[Category: Maclachlan B]]
[[Category: Rossjohn J]]
[[Category: Rossjohn J]]
[[Category: Vivian JP]]
[[Category: Vivian JP]]

Latest revision as of 14:19, 30 October 2024

HLA-B*57:01 presenting the peptide ASLNLPAVSWHLA-B*57:01 presenting the peptide ASLNLPAVSW

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.27Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

6v2o, resolution 1.27Å

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