View source for 9l48


==Crystal structure of HLA-C*12:02-RV9==
<StructureSection load='9l48' size='340' side='right'caption='[[9l48]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9l48]] is a 3 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=9L48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9L48 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]] 1.9&#8491;</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=9l48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9l48 OCA], [https://pdbe.org/9l48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9l48 RCSB], [https://www.ebi.ac.uk/pdbsum/9l48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9l48 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S5DHS4_HUMAN S5DHS4_HUMAN] Involved in the presentation of foreign antigens to the immune system.[ARBA:ARBA00002297]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Micropolymorphisms drastically shape the antigen presentation characteristics of human leukocyte antigen class I (HLA-I) molecules, with profound implications for immune responses and disease susceptibility. HLA-C*12:02 and HLA-C*12:03 are closely related HLA-I allotypes that differ by a single amino acid substitution (R97W) but exhibit distinct associations with disease. HLA-C*12:02 has been shown to provide protective effects against HIV infection, playing a crucial role in controlling viral replication and slowing disease progression, whereas HLA-C*12:03 is associated with increased susceptibility to psoriasis. We determined the X-ray crystal structures of the two allotypes presenting MARELHPEY (MY9) and RAFPGLRYV (RV9). Peptide residues that function as anchors, as well as those accessible for T-cell antigen receptor (TCR) contact, were identified. Our results, combined with those of biochemical studies, demonstrated that the R97W variation alters the peptide-binding groove (PBG) volume and charge, leading to conformational and stability changes in pHLA-C*12 complexes and ultimately affecting peptide-binding preferences for the two HLA-C*12 allotypes. This research not only advances our understanding of the impact of HLA-I micropolymorphisms but also offers clues for the use of structure-guided therapeutics to interfere with peptide binding.

Biochemical and structural insights into position 97 micropolymorphisms in human leukocyte antigen (HLA)-C*12 allotypes and their differential disease associations.,Yang M, Zhong P, Liu Q, Jiao H, Lei J, Wei P Int J Biol Macromol. 2025 Mar 6;306(Pt 3):141681. doi: , 10.1016/j.ijbiomac.2025.141681. PMID:40044006<ref>PMID:40044006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9l48" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Wei PC]]
[[Category: Yang M]]
[[Category: Zhong PL]]