1BX2

CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101,DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN

Summary for 1BX2

• Entry DOI: 10.2210/pdb1bx2/pdb
• Descriptor: PROTEIN (HLA-DR2), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: hla-dr2, myelin basic protein, multiple sclerosis, autoimmunity, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 90619.79

Authors

Smith, K.J.,Pyrdol, J.,Gauthier, L.,Wiley, D.C.,Wucherpfennig, K. (deposition date: 1998-10-12, release date: 1998-10-21, Last modification date: 2024-11-13)

Primary citation

Smith, K.J.,Pyrdol, J.,Gauthier, L.,Wiley, D.C.,Wucherpfennig, K.W.
Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein.
J.Exp.Med., 188:1511-1520, 1998

PubMed Abstract: Susceptibility to multiple sclerosis is associated with the human histocompatibility leukocyte antigen (HLA)-DR2 (DRB1*1501) haplotype. The structure of HLA-DR2 was determined with a bound peptide from human myelin basic protein (MBP) that is immunodominant for human MBP-specific T cells. Residues of MBP peptide that are important for T cell receptor recognition are prominent, solvent exposed residues in the crystal structure. A distinguishing feature of the HLA-DR2 peptide binding site is a large, primarily hydrophobic P4 pocket that accommodates a phenylalanine of the MBP peptide. The necessary space for this aromatic side chain is created by an alanine at the polymorphic DRbeta 71 position. These features make the P4 pocket of HLA-DR2 distinct from DR molecules associated with other autoimmune diseases.

PubMed: 9782128
DOI: 10.1084/jem.188.8.1511

Experimental method

X-RAY DIFFRACTION (2.6 Å)