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Review
. 1998 Jun:163:129-38.
doi: 10.1111/j.1600-065x.1998.tb01192.x.

Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G

C A O'Callaghan  1 , J I Bell
Affiliations
Review

Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G

C A O'Callaghan et al. Immunol Rev. 1998 Jun.

Abstract

The major histocompatibility (MHC) class Ib molecules HLA-E, HLA-F and HLA-G are relatively non-polymorphic compared to class Ia molecules. Both HLA-E and HLA-G bind peptides and are involved in natural killer (NK)-cell recognition, but the role of HLA-F is unclear. HLA-E binds specifically to the conserved leader sequence peptides from the class Ia MHC molecules and interacts on the cell surface with the CD94/NKG2 class of NK-cell receptors. The framework structure of HLA-E is similar to that of the MHC class Ia molecules, but the peptide-binding groove is highly adapted for the specific binding of the leader sequence peptides. This is different from class Ia molecules, which have highly promiscuous peptide-binding grooves. The HLA-E groove makes full use of all the available pockets and imposes specificity along the entire length of the peptide. HLA-G binds nonamer peptides with leucine or isoleucine at position 2, proline at position 3 and leucine at position 9. Expression of HLA-G inhibits NK cells expressing the CD94/NKG2 class of receptors, though an interaction with these receptors has not been directly demonstrated.

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