5DEF

Crystal structure of B*27:04 complex bound to the pVIPR peptide

Summary for 5DEF

• Entry DOI: 10.2210/pdb5def/pdb
• Related: 1OF2 1OGT
• Descriptor: HLA class I histocompatibility antigen, B-27 alpha chain, Beta-2-microglobulin, peptide derived from VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1 (pVIPR), ... (6 entities in total)
• Functional Keywords: immune system-complex, immune system, mhc major histocompatibility complex), hla- b*2704
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 45598.98

Authors

Loll, B.,Fabian, H.,Huser, H.,Hee, C.S.,Uchanska-Ziegler, B.,Ziegler, A. (deposition date: 2015-08-25, release date: 2015-11-18, Last modification date: 2024-10-23)

Primary citation

Loll, B.,Fabian, H.,Huser, H.,Hee, C.S.,Ziegler, A.,Uchanska-Ziegler, B.,Ziegler, A.
Increased Conformational Flexibility of HLA-B*27 Subtypes Associated With Ankylosing Spondylitis.
Arthritis Rheumatol, 68:1172-1182, 2016

PubMed Abstract: Dissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA-B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this notion, previous x-ray crystallographic data showed that peptides can be displayed by almost identical HLA-B*27 molecules in a subtype-dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, a human self-peptide derived from vasoactive intestinal peptide receptor type 1 (pVIPR; sequence RRKWRRWHL) is displayed in a single conformation by B*27:09 (which is not associated with AS), while B*27:05 (which is associated with AS) presents the peptide in a dual binding mode. In addition, differences in conformational flexibility between these subtypes might affect their stability or antigen presentation capability. This study was undertaken to investigate B*27:04 and B*27:06, another pair of minimally distinct HLA-B*27 subtypes, to assess whether dual peptide conformations or structural dynamics play a role in the initiation of AS.

PubMed: 26748477
DOI: 10.1002/art.39567

Experimental method

X-RAY DIFFRACTION (1.6 Å)