Title : NK cell inhibitory receptor Ly-49C residues involved in MHC class I binding.

Pub. Date : 2002 Jan 15

PMID : 11777974






4 Functional Relationships(s)
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1 The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts. Lysine major histocompatibility complex, class I, C Homo sapiens
2 The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts. Lysine major histocompatibility complex, class I, C Homo sapiens
3 The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts. Lysine major histocompatibility complex, class I, C Homo sapiens
4 The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts. Lysine major histocompatibility complex, class I, C Homo sapiens