1K5N

HLA-B*2709 BOUND TO NONA-PEPTIDE M9

Summary for 1K5N

• Entry DOI: 10.2210/pdb1k5n/pdb
• Related: 1hsa 1jgd 1jge
• Descriptor: major histocompatibility complex molecule HLA-B*2709, beta-2-microglobulin, light chain, nonameric model peptide m9, ... (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: P61769
• Total number of polymer chains: 3
• Total formula weight: 44920.85

Authors

Hulsmeyer, M.,Hillig, R.C.,Volz, A.,Ruhl, M.,Schroder, W.,Saenger, W.,Ziegler, A.,Uchanska-Ziegler, B. (deposition date: 2001-10-11, release date: 2002-10-30, Last modification date: 2024-10-30)

Primary citation

Hulsmeyer, M.,Hillig, R.C.,Volz, A.,Ruhl, M.,Schroder, W.,Saenger, W.,Ziegler, A.,Uchanska-Ziegler, B.
HLA-B27 Subtypes Differentially Associated with Disease Exhibit Subtle Structural Alterations
J.Biol.Chem., 277:47844-47853, 2002

PubMed Abstract: The reasons for the association of the human major histocompatibility complex protein HLA-B27 with spondyloarthropathies are unknown. To uncover the underlying molecular causes, we determined the crystal structures of the disease-associated B*2705 and the nonassociated B*2709 subtypes complexed with the same nonapeptide (GRFAAAIAK). Both differ in only one residue (Asp(116) and His(116), respectively) in the F-pocket that accommodates the peptide C terminus. Several different effects of the Asp(116) --> His replacement are observed. The bulkier His(116) induces a movement of peptide C-terminal pLys(9), allowing the formation of a novel salt bridge to Asp(77), whereas the salt bridge between pLys(9) and Asp(116) is converted into a hydrogen bond with His(116). His(116) but not Asp(116) adopts two alternative conformations, one of which leads to breakage of hydrogen bonds. Water molecules near residue 116 differ with regard to number, position, and contacts made. Furthermore, F-pocket atoms exhibit higher B-factors in B*2709 than in B*2705, indicating an increased flexibility of the entire region in the former subtype. These changes induce subtle peptide conformational alterations that may be responsible for the immunobiological differences between these HLA-B27 subtypes.

PubMed: 12244049
DOI: 10.1074/jbc.M206392200

Experimental method

X-RAY DIFFRACTION (1.09 Å)