Selected article for: "heavy chain and Î sheet"

Author: Jones, Harrison G.; Battles, Michael B.; Lin, Chun-Chi; Bianchi, Siro; Corti, Davide; McLellan, Jason S.
Title: Alternative conformations of a major antigenic site on RSV F
  • Document date: 2019_7_15
  • ID: 1r20hl2b_14
    Snippet: Sequence comparison of the two RSV F subtypes demonstrates that the residues comprising the AM22 epitope are well-conserved. However, one of the subtype A RSV F residues that contacts AM22 is Lys209, which is a Gln in subtype B (Fig 2C) . The Lys209 side chain of subtype A prefusion RSV F is coordinated by three residues of the AM22 heavy chain. This includes the formation of a salt bridge with Asp100G of the CDR H3 that effectively extends the p.....
    Document: Sequence comparison of the two RSV F subtypes demonstrates that the residues comprising the AM22 epitope are well-conserved. However, one of the subtype A RSV F residues that contacts AM22 is Lys209, which is a Gln in subtype B (Fig 2C) . The Lys209 side chain of subtype A prefusion RSV F is coordinated by three residues of the AM22 heavy chain. This includes the formation of a salt bridge with Asp100G of the CDR H3 that effectively extends the prominent β-sheet interaction. Substitution of Lys209 with Gln, as found in subtype B, would eliminate the salt bridge and may explain the subtype A preference of AM22. Indeed, incorporating

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