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Literature DB >> 12445302

HLA-B27 and the pathogenesis of spondyloarthritis.

Abstract

The association of HLA-B27 with ankylosing spondylitis and other spondyloarthropathies ranks among the strongest between any HLA antigen and a human disease. Yet, in spite of intense research and advanced knowledge of the biochemistry and biology of major histocompatibility complex molecules, the mechanism of this association remains unknown. This review attempts a critical assessment of current pathogenetic hypotheses from evidence concerning the epidemiology of HLA-B27 association with disease, its peptide-binding specificity, and other aspects of the molecular biology and immunology of this molecule.

Entities: Disease Gene Species

Mesh：

Substances：
HLA-B27 Antigen

Year: 2002 PMID： 12445302 DOI： 10.1034/j.1399-0039.2002.600301.x

Source DB: PubMed Journal: Tissue Antigens ISSN： 0001-2815

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Cited

20 in total

1. A single residue exchange between two HLA-B27 alleles triggers increased peptide flexibility.

Authors: Ewgeni B Starikov; Ewgeni B Starikow; Lennart Nilsson; Martin Hülsmeyer
Journal: Eur Biophys J Date: 2004-03-10 Impact factor: 1.733

2. Loss of recognition by cross-reactive T cells and its relation to a C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide.

Authors: Bernhard Loll; Christine Rückert; Chee Seng Hee; Wolfram Saenger; Barbara Uchanska-Ziegler; Andreas Ziegler
Journal: Protein Sci Date: 2010-12-23 Impact factor: 6.725

3. X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide.

Authors: Anna Zawacka; Bernhard Loll; Jacek Biesiadka; Wolfram Saenger; Barbara Uchanska-Ziegler; Andreas Ziegler
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2005-11-24

4. Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide.

Authors: Bernhard Loll; Anna Zawacka; Jacek Biesiadka; Cordula Petter; Christine Rückert; Wolfram Saenger; Barbara Uchanska-Ziegler; Andreas Ziegler
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2005-09-30

5. Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide.

Authors: Bernhard Loll; Anna Zawacka; Jacek Biesiadka; Christine Rückert; Armin Volz; Wolfram Saenger; Barbara Uchanska-Ziegler; Andreas Ziegler
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2005-03-12

6. Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral peptide and with a self-peptide.

Authors: Pravin Kumar; Ardeschir Vahedi-Faridi; Elena Merino; José A López de Castro; Armin Volz; Andreas Ziegler; Wolfram Saenger; Barbara Uchanska-Ziegler
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2007-06-29

HLA-B27 and the pathogenesis of spondyloarthritis.

1. A single residue exchange between two HLA-B27 alleles triggers increased peptide flexibility.

2. Loss of recognition by cross-reactive T cells and its relation to a C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide.

3. X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide.

4. Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide.

5. Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide.

6. Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral peptide and with a self-peptide.

Review 7. The synovio-entheseal complex in enthesoarthritis.

8. Natural MHC class I polymorphism controls the pathway of peptide dissociation from HLA-B27 complexes.

9. High frequencies of HLA-B27 in Chinese patients with suspected of ankylosing spondylitis.

10. Structural basis for T cell alloreactivity among three HLA-B14 and HLA-B27 antigens.