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 Cited by 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: 9782128DOI: 10.1084/jem.188.8.1511 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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