The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation.

[1]  D. Zaller,et al.  Secondary Structure Composition and pH-dependent Conformational Changes of Soluble Recombinant HLA-DM* , 1998, The Journal of Biological Chemistry.

[2]  R. Doebele,et al.  Novel glycosylation of HLA-DRalpha disrupts antigen presentation without altering endosomal localization. , 1998, Journal of immunology.

[3]  P. A. Peterson,et al.  Altered antigen presentation in mice lacking H2-O. , 1998, Immunity.

[4]  R. Doebele,et al.  Aberrant intermolecular disulfide bonding in a mutant HLA-DM molecule: implications for assembly, maturation, and function. , 1998, Journal of immunology.

[5]  J. Trowsdale,et al.  HLA-DO is a negative modulator of HLA-DM-mediated MHC class II peptide loading , 1997, Current Biology.

[6]  J. Trowsdale,et al.  Interaction between HLA-DM and HLA-DR involves regions that undergo conformational changes at lysosomal pH. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[7]  P. Cresswell,et al.  Negative regulation by HLA-DO of MHC class II-restricted antigen processing. , 1997, Science.

[8]  D. Zaller,et al.  X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. , 1997, Immunity.

[9]  P. A. Peterson,et al.  Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove. , 1997, Science.

[10]  G. Hämmerling,et al.  HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH. , 1997, Immunity.

[11]  D. Douek,et al.  HLA-DO is an intracellular class II molecule with distinctive thymic expression. , 1997, International immunology.

[12]  P. Cresswell,et al.  HLA-DM Interactions with Intermediates in HLA-DR Maturation and a Role for HLA-DM in Stabilizing Empty HLA-DR Molecules , 1996, The Journal of experimental medicine.

[13]  B. Evavold,et al.  Enhanced Dissociation of HLA-DR-Bound Peptides in the Presence of HLA-DM , 1996, Science.

[14]  M. Jackson,et al.  HLA‐DO is a lysosomal resident which requires association with HLA‐DM for efficient intracellular transport. , 1996, The EMBO journal.

[15]  D. Fremont,et al.  Structures of an MHC Class II Molecule with Covalently Bound Single Peptides , 1996, Science.

[16]  P. Cresswell.  Invariant Chain Structure and MHC Class II Function , 1996, Cell.

[17]  R. Busch,et al.  Developing and shedding inhibitions: how MHC class II molecules reach maturity. , 1996, Current opinion in immunology.

[18]  Partho Ghosh,et al.  The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3 , 1995, Nature.

[19]  D. Wiley,et al.  Invariant chain made in Escherichia coli has an exposed N-terminal segment that blocks antigen binding to HLA-DR1 and a trimeric C-terminal segment that binds empty HLA-DR1. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[20]  D. Weber,et al.  DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. , 1995, Immunity.

[21]  P. Cresswell,et al.  HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading , 1995, Cell.

[22]  D. Zaller,et al.  Mediation by HLA-DM of dissociation of peptides from HLA-DR , 1995, Nature.

[23]  Janet L. Schottel,et al.  A novel variant of the catalytic triad in the Streptomyces scabies esterase , 1995, Nature Structural Biology.

[24]  D. Wiley,et al.  Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1. , 1994, Science.

[25]  S. Porcelli,et al.  Recognition of a lipid antigen by GDI-restricted αβ+ T cells , 1994, Nature.

[26]  P. Bjorkman,et al.  Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor , 1994, Nature.

[27]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[28]  Don C. Wiley,et al.  Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen , 1994, Nature.

[29]  B. Arp,et al.  HLA-DMA and -DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells , 1994, Nature.

[30]  Jeffrey A. Shaman,et al.  An essential role for HLA–DM in antigen presentation by class II major histocompatibility molecules , 1994, Nature.

[31]  Don C. Wiley,et al.  Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide , 1994, Nature.

[32]  L. Smith,et al.  A mutant human histocompatibility leukocyte antigen DR molecule associated with invariant chain peptides , 1994, The Journal of experimental medicine.

[33]  D. Wiley,et al.  Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 , 1993, Nature.

[34]  R. Germain,et al.  Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes surface expression of occupied molecules , 1993, Nature.

[35]  S. Ceman,et al.  Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant. , 1992, Science.

[36]  P. Cresswell,et al.  HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides , 1992, Nature.

[37]  D. Wiley,et al.  The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide , 1992, Cell.

[38]  John Trowsdale,et al.  A new human HLA class II-related locus, DM , 1991, Nature.

[39]  J. Monaco,et al.  New class ll-like genes in the murine MHC , 1991, Nature.

[40]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[41]  A T Brünger,et al.  Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.

[42]  H. Grey,et al.  Autologous peptides constitutively occupy the antigen binding site on Ia. , 1988, Science.

[43]  A Sette,et al.  The Interaction between Protein‐Derived Immunogenic Peptides and Ia , 1987, Immunological reviews.

[44]  T. Watts,et al.  High-affinity fluorescent peptide binding to I-Ad in lipid membranes. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[45]  Eric O Long,et al.  DO beta: a new beta chain gene in HLA‐D with a distinct regulation of expression. , 1985, The EMBO journal.

[46]  J. Trowsdale,et al.  The human HLA class II alpha chain gene DZ alpha is distinct from genes in the DP, DQ and DR subregions. , 1985, The EMBO journal.

[47]  J. Trowsdale,et al.  Association between HLA-DM and HLA-DR in vivo. , 1996, Immunity.

[48]  H. Ploegh,et al.  How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. , 1995, Annual review of cell and developmental biology.

[49]  P. Cresswell,et al.  Assembly, transport, and function of MHC class II molecules. , 1994, Annual review of immunology.

[50]  Axel T. Brunger,et al.  X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .