3KYN

Crystal structure of HLA-G presenting KGPPAALTL peptide

Summary for 3KYN

• Entry DOI: 10.2210/pdb3kyn/pdb
• Related: 1YDB 2D31 2DYP 3KYO
• Descriptor: MHC class I antigen, Beta-2-microglobulin, KGPPAALTL peptide, ... (6 entities in total)
• Functional Keywords: human leukocyte antigen, major histocompatibility complex, immune response, mhc i, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 44738.63

Authors

Walpole, N.G.,Rossjohn, J.,Clements, C.S. (deposition date: 2009-12-06, release date: 2010-02-23, Last modification date: 2023-11-01)

Primary citation

Walpole, N.G.,Kjer-Nielsen, L.,Kostenko, L.,McCluskey, J.,Brooks, A.G.,Rossjohn, J.,Clements, C.S.
The structure and stability of the monomorphic HLA-G are influenced by the nature of the bound peptide
J.Mol.Biol., 397:467-480, 2010

PubMed Abstract: The highly polymorphic major histocompatibility complex class Ia (MHC-Ia) molecules present a broad array of peptides to the clonotypically diverse alphabeta T-cell receptors. In contrast, MHC-Ib molecules exhibit limited polymorphism and bind a more restricted peptide repertoire, in keeping with their major role in innate immunity. Nevertheless, some MHC-Ib molecules do play a role in adaptive immunity. While human leukocyte antigen E (HLA-E), the MHC-Ib molecule, binds a very restricted repertoire of peptides, the peptide binding preferences of HLA-G, the class Ib molecule, are less stringent, although the basis by which HLA-G can bind various peptides is unclear. To investigate how HLA-G can accommodate different peptides, we compared the structure of HLA-G bound to three naturally abundant self-peptides (RIIPRHLQL, KGPPAALTL and KLPQAFYIL) and their thermal stabilities. The conformation of HLA-G(KGPPAALTL) was very similar to that of the HLA-G(RIIPRHLQL) structure. However, the structure of HLA-G(KLPQAFYIL) not only differed in the conformation of the bound peptide but also caused a small shift in the alpha2 helix of HLA-G. Furthermore, the relative stability of HLA-G was observed to be dependent on the nature of the bound peptide. These peptide-dependent effects on the substructure of the monomorphic HLA-G are likely to impact on its recognition by receptors of both innate and adaptive immune systems.

PubMed: 20122941
DOI: 10.1016/j.jmb.2010.01.052

Experimental method

X-RAY DIFFRACTION (2.4 Å)