1JGD

HLA-B*2709 bound to deca-peptide s10R

Summary for 1JGD

• Entry DOI: 10.2210/pdb1jgd/pdb
• Related: 1hsa 1jge 1k5n
• Descriptor: HUMAN LYMPHOCYTE ANTIGEN HLA-B27, BETA-2-MICROGLOBULIN, peptide s10R, ... (5 entities in total)
• Functional Keywords: mhc (major histocompatibility complex), hla (human leukocyte antigen), immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P03989; Secreted . Note=(Microbial infection) In the presence of M: P61769
• Total number of polymer chains: 3
• Total formula weight: 45239.18

Authors

Hillig, R.C.,Huelsmeyer, M.,Saenger, W.,Volz, A.,Uchanska-Ziegler, B.,Ziegler, A. (deposition date: 2001-06-25, release date: 2003-07-01, Last modification date: 2024-10-09)

Primary citation

Hillig, R.C.,Huelsmeyer, M.,Saenger, W.,Welfle, K.,Misselwitz, R.,Welfle, H.,Kozerski, C.,Volz, A.,Uchanska-Ziegler, B.,Ziegler, A.
Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association
J.Biol.Chem., 279:652-663, 2004

PubMed Abstract: Selected HLA-B27 subtypes are associated with spondyloarthropathies, but the underlying mechanism is not understood. To explain this association in molecular terms, a comparison of peptide-dependent dynamic and structural properties of the differentially disease-associated subtypes HLA-B*2705 and HLA-B*2709 was carried out. These molecules differ only by a single amino acid at the floor of the peptide binding groove. The thermostabilities of a series of HLA-B27 molecules complexed with nonameric and decameric peptides were determined and revealed substantial differences depending on the subtype as well as the residues at the termini of the peptides. In addition we present the crystal structure of the B*2709 subtype complexed with a decameric peptide. This structure provides an explanation for the preference of HLA-B27 for a peptide with an N-terminal arginine as secondary anchor and the lack of preference for tyrosine as peptide C terminus in B*2709. The data show that differences in thermodynamic properties between peptide-complexed HLA-B27 subtypes are correlated with a variety of structural properties.

PubMed: 14555655
DOI: 10.1074/jbc.M307457200

Experimental method

X-RAY DIFFRACTION (1.9 Å)