TcR recognition of the MHC-peptide dimer: Structural properties of a ternary complex

Vasmatzis G., Cornette J., Sezerman U., DeLisi C.

JOURNAL OF MOLECULAR BIOLOGY, cilt.261, sa.1, ss.72-89, 1996 (SCI-Expanded) identifier identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 261 Sayı: 1
  • Basım Tarihi: 1996
  • Doi Numarası: 10.1006/jmbi.1996.0442
  • Dergi Adı: JOURNAL OF MOLECULAR BIOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.72-89
  • Anahtar Kelimeler: T-cell receptor, class I MHC, ternary complex, local moves, TcR-MHC orientation, CELL ANTIGEN RECEPTOR, ANTIBODY HYPERVARIABLE LOOPS, CRYSTAL-STRUCTURE, BETA-CHAIN, REGIONS, BINDING, CONFORMATIONS, SPECIFICITY, ALGORITHM, ENERGIES
  • Acıbadem Mehmet Ali Aydınlar Üniversitesi Adresli: Hayır

Özet

We have developed a method that utilizes site-specific mutation data, sequence analysis, immunological data and free-energy minimization, to determine structural features of the ternary complex formed by the T-cell receptor (TcR) and the class I major histocompatibility complex (MHC) molecule bound by peptide. The analysis focuses on the mouse Kd MHC system, for which a large set of clones with sequenced T-cell receptors is available for specific peptides.