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'''Unreleased structure'''


The entry 24st is ON HOLD
==Crystal Structure of the cross-restricted 14D7 TCR and HLA-B*81:01 bound to HIV-1 Gag TL9 peptide==
<StructureSection load='24st' size='340' side='right'caption='[[24st]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[24st]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(WMJ2_ISOLATE) Human immunodeficiency virus type 1 (WMJ2 ISOLATE)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=24ST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=24ST 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]] 2.7&#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=24st FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=24st OCA], [https://pdbe.org/24st PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=24st RCSB], [https://www.ebi.ac.uk/pdbsum/24st PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=24st 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/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 ==
Dual-reactive T cell receptors (TCRs) that recognize the HIV-1 Gag TL9 epitope presented by both HLA-B*81:01 and HLA-B*42:01 are associated with improved immune control. However, whether such TCRs rely on a single universal recognition blueprint or adopt distinct structural solutions remains unclear. Here, we characterize 14D7, an additional dual-reactive TL9-specific TCR, and compare its structural features with those of the previously reported T18A clonotype. The 14D7-HLA-B*81:01-TL9 structure reveals a conserved non-canonical recognition framework shared with T18A: in both TCRs, CDR3beta primarily engages the HLA alpha2 helix rather than the peptide, while CDR2beta compensates via critical peptide contacts. However, 14D7 adopts a distinct CDR3 loop conformation, likely reflecting differences in V/J gene usage and junctional rearrangement, demonstrating that dual-reactive TCRs can achieve cross-reactivity through related but non-identical molecular solutions. AlphaFold 3 modeling further suggests that, like T18A, 14D7 actively remodels the TL9 conformation in the HLA-B*42:01 context toward a state resembling that observed in the HLA-B*81:01-bound complex. Surface plasmon resonance analysis revealed differential affinity profiles across HLA backgrounds, with greater tolerance to common escape variants in the HLA-B*81:01 context. Structural comparison further suggests that polymorphic HLA residues, particularly at positions 143 and 163, reshape the peptide- and TCR-facing interaction network and thereby influence tolerance to epitope variation. Together, these findings show that dual-reactive TCRs operate within a conserved non-canonical recognition framework while retaining flexibility at the level of CDR3 loop configuration, providing a refined structural basis for HIV-specific cross-reactive T cell immunity.


Authors:  
Conserved non-canonical recognition with distinct structural solutions underlies dual-HLA recognition of HIV-1 Gag TL9.,Meng J, Lei J, Wei Q, Wei P Int J Biol Macromol. 2026 Jun;369:152866. doi: 10.1016/j.ijbiomac.2026.152866. , Epub 2026 Jun 1. PMID:42229649<ref>PMID:42229649</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 24st" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Meng JQ]]
[[Category: Wei PC]]
Retrieved from "https://proteopedia.org/24st"