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PDBsum entry 3vxs
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Immune system
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PDB id
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3vxs
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Contents |
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274 a.a.
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100 a.a.
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204 a.a.
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242 a.a.
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PDB id:
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| Name: |
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Immune system
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Title:
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The complex between h27-14 tcr and hla-a24 bound to HIV-1 nef134- 10(6l) peptide
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Structure:
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Hla class i histocompatibility antigen, a-24 alpha chain. Chain: a. Fragment: unp residues 25-298. Synonym: aw-24, hla class i histocompatibility antigen, a-9 alpha chain, mhc class i antigen a 24. Engineered: yes. Beta-2-microglobulin. Chain: b. Synonym: beta-2-microglobulin form pi 5.3.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-a. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b2m. Synthetic: yes. Human immunodeficiency virus 1.
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Resolution:
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1.80Å
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R-factor:
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0.203
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R-free:
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0.230
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Authors:
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A.Shimizu,S.Fukai,A.Yamagata,A.Iwamoto
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Key ref:
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A.Shimizu
et al.
(2013).
Structure of TCR and antigen complexes at an immunodominant CTL epitope in HIV-1 infection.
Sci Rep,
3,
3097.
PubMed id:
DOI:
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Date:
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20-Sep-12
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Release date:
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23-Oct-13
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PROCHECK
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Headers
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References
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P04439
(1A03_HUMAN) -
HLA class I histocompatibility antigen, A alpha chain from Homo sapiens
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Seq:
Struc:
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365 a.a.
274 a.a.*
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P61769
(B2MG_HUMAN) -
Beta-2-microglobulin from Homo sapiens
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Seq:
Struc:
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119 a.a.
100 a.a.*
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DOI no:
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Sci Rep
3:3097
(2013)
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PubMed id:
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Structure of TCR and antigen complexes at an immunodominant CTL epitope in HIV-1 infection.
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A.Shimizu,
A.Kawana-Tachikawa,
A.Yamagata,
C.Han,
D.Zhu,
Y.Sato,
H.Nakamura,
T.Koibuchi,
J.Carlson,
E.Martin,
C.J.Brumme,
Y.Shi,
G.F.Gao,
Z.L.Brumme,
S.Fukai,
A.Iwamoto.
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ABSTRACT
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We investigated the crystal structure of an HLA-A*2402-restricted CTL epitope in
the HIV-1 nef gene (Nef134-10) before (pHLA) or after TCR docking. The wild type
epitope and two escape mutants were included in the study. Y135F was an
early-appearing major mutation, while F139L was a late-appearing mutation which
was selected in the patients without Y135F. F139 was an eminent feature of the
Nef134-10 epitope. Wild type-specific TCR was less fit to F139L mutant
suggesting that F139L is an escape from the CTL against the wild type epitope.
Although Y135F mutation disrupted the hydrogen bond to HLA-A*2402 His70, newly
formed hydrogen bond between T138 and His70 kept the conformation of the epitope
in the reconstituted pMHC. TCR from Y135F- or dually-specific CTL had unique
mode of binding to the mutant epitope. Y135F has been reported as a processing
mutant but CTL carrying structurally adequate TCR can be found in the patients.
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Links
