The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC - PubMed (original) (raw)
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC
D R Madden et al. Cell. 1992.
Abstract
Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
Similar articles
- Covalent HLA-B27/peptide complex induced by specific recognition of an aziridine mimic of arginine.
Weiss GA, Valentekovich RJ, Collins EJ, Garboczi DN, Lane WS, Schreiber SL, Wiley DC. Weiss GA, et al. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10945-8. doi: 10.1073/pnas.93.20.10945. Proc Natl Acad Sci U S A. 1996. PMID: 8855288 Free PMC article. - Gorillas with spondyloarthropathies express an MHC class I molecule with only limited sequence similarity to HLA-B27 that binds peptides with arginine at P2.
Urvater JA, Hickman H, Dzuris JL, Prilliman K, Allen TM, Schwartz KJ, Lorentzen D, Shufflebotham C, Collins EJ, Neiffer DL, Raphael B, Hildebrand W, Sette A, Watkins DI. Urvater JA, et al. J Immunol. 2001 Mar 1;166(5):3334-44. doi: 10.4049/jimmunol.166.5.3334. J Immunol. 2001. PMID: 11207289 Review. - Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding.
Parker KC, Biddison WE, Coligan JE. Parker KC, et al. Biochemistry. 1994 Jun 21;33(24):7736-43. doi: 10.1021/bi00190a029. Biochemistry. 1994. PMID: 8011638 - Unusual topology of an HLA-B27 allospecific T cell epitope lacking peptide specificity.
Villadangos JA, Galocha B, López de Castro JA. Villadangos JA, et al. J Immunol. 1994 Mar 1;152(5):2317-23. J Immunol. 1994. PMID: 7510742 - Immunogenetics of spondyloarthropathies.
Khan MA, Kellner H. Khan MA, et al. Rheum Dis Clin North Am. 1992 Nov;18(4):837-64. Rheum Dis Clin North Am. 1992. PMID: 1455047 Review.
Cited by
- HLA-B*27 and Ankylosing Spondylitis: 50 Years of Insights and Discoveries.
Khan MA. Khan MA. Curr Rheumatol Rep. 2023 Dec;25(12):327-340. doi: 10.1007/s11926-023-01118-5. Curr Rheumatol Rep. 2023. PMID: 37950822 Review. - Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide.
Hadeler A, Saikia A, Zacharias M, Springer S. Hadeler A, et al. Curr Res Immunol. 2022 Aug 18;3:167-174. doi: 10.1016/j.crimmu.2022.08.002. eCollection 2022. Curr Res Immunol. 2022. PMID: 36042776 Free PMC article. - A short HLA-DRA isoform binds the HLA-DR2 heterodimer on the outer domain of the peptide-binding site.
Shams H, Hollenbach JA, Matsunaga A, Mofrad MRK, Oksenberg JR, Didonna A. Shams H, et al. Arch Biochem Biophys. 2022 Apr 15;719:109156. doi: 10.1016/j.abb.2022.109156. Epub 2022 Feb 24. Arch Biochem Biophys. 2022. PMID: 35218721 Free PMC article. - 50 Years of structural immunology.
Wilson IA, Stanfield RL. Wilson IA, et al. J Biol Chem. 2021 Jan-Jun;296:100745. doi: 10.1016/j.jbc.2021.100745. Epub 2021 May 3. J Biol Chem. 2021. PMID: 33957119 Free PMC article. Review. - Beyond history and "on a roll": The list of the most well-studied human protein structures and overall trends in the protein data bank.
Li ZL, Buck M. Li ZL, et al. Protein Sci. 2021 Apr;30(4):745-760. doi: 10.1002/pro.4038. Epub 2021 Mar 4. Protein Sci. 2021. PMID: 33550681 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials