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

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 c...

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Main Authors: O'Callaghan, C, Bell, J
Format: Journal article
Language:English
Published: 1998
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author O'Callaghan, C
Bell, J
author_facet O'Callaghan, C
Bell, J
author_sort O'Callaghan, C
collection OXFORD
description 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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spelling oxford-uuid:8659e8da-02ab-46b7-bb35-c838b0c3563d2022-03-26T22:03:26ZStructure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8659e8da-02ab-46b7-bb35-c838b0c3563dEnglishSymplectic Elements at Oxford1998O'Callaghan, CBell, JThe 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.
spellingShingle O'Callaghan, C
Bell, J
Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title_full Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title_fullStr Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title_full_unstemmed Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title_short Structure and function of the human MHC class Ib molecules HLA-E, HLA-F and HLA-G.
title_sort structure and function of the human mhc class ib molecules hla e hla f and hla g
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