메뉴 건너뛰기




Volumn 93, Issue 8, 2007, Pages 2743-2755

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; BETAINE; GLYCYLARGINYLPHENYLALANYLALANYLALANYLALANYLISOLEUCYLALANYLLYSINE; HLA B27 ANTIGEN; HLA B2705 ANTIGEN; HLA B2709 ANTIGEN; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 35348937601     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.096602     Document Type: Article
Times cited : (31)

References (31)
  • 1
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden, D. R. 1995. The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13:587-622.
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 2
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer, E., and P. Cresswell. 1998. Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16:323-358.
    • (1998) Annu. Rev. Immunol , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 3
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper, M. A., P. J. Bjorkman, and D. C. Wiley. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:277-319.
    • (1991) J. Mol. Biol , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 5
    • 0037129952 scopus 로고    scopus 로고
    • Update on spondyloarthropathies
    • Khan, M. A. 2002. Update on spondyloarthropathies. Ann. Intern. Med. 136:896-907.
    • (2002) Ann. Intern. Med , vol.136 , pp. 896-907
    • Khan, M.A.1
  • 6
    • 18744386087 scopus 로고    scopus 로고
    • HLA-B27 and the pathogenesis of spondyloarthritis
    • Ramos, M., and J. A. López de Castro. 2002. HLA-B27 and the pathogenesis of spondyloarthritis. Tissue Antigens. 60:191-205.
    • (2002) Tissue Antigens , vol.60 , pp. 191-205
    • Ramos, M.1    López de Castro, J.A.2
  • 7
    • 23044441334 scopus 로고    scopus 로고
    • Pathogenesis of ankylosing spondylitis and reactive arthritis
    • Kim, T.-H., W.-S. Uhm, and R. D. Inman. 2005. Pathogenesis of ankylosing spondylitis and reactive arthritis. Curr. Opin. Rheumatol. 17:400-405.
    • (2005) Curr. Opin. Rheumatol , vol.17 , pp. 400-405
    • Kim, T.-H.1    Uhm, W.-S.2    Inman, R.D.3
  • 10
    • 0028924745 scopus 로고
    • 116 substitution in a novel HLA-B27 subtype influences the acceptance of the peptide C-terminal anchor
    • 116 substitution in a novel HLA-B27 subtype influences the acceptance of the peptide C-terminal anchor. Immunogenetics. 41:38-39.
    • (1995) Immunogenetics , vol.41 , pp. 38-39
    • Fiorillo, M.T.1    Greco, G.2    Sorrentino, R.3
  • 11
    • 0037047424 scopus 로고    scopus 로고
    • Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability
    • Ramos, M., A. Paradela, M. Vázquez, A. Marina, J. Vázquez, and J. A. López de Castro. 2002. Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability. J. Biol. Chem. 277:28749-28756.
    • (2002) J. Biol. Chem , vol.277 , pp. 28749-28756
    • Ramos, M.1    Paradela, A.2    Vázquez, M.3    Marina, A.4    Vázquez, J.5    López de Castro, J.A.6
  • 15
    • 0038670730 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analysis of a peptide-class I MHC interaction highlights the noncovalent nature and conformational dynamics of the class I heterotrimer
    • Binz, A.-K., R. C. Rodriguez, W. E. Biddison, and B. M. Baker. 2003. Thermodynamic and kinetic analysis of a peptide-class I MHC interaction highlights the noncovalent nature and conformational dynamics of the class I heterotrimer. Biochemistry. 42:4954-4961.
    • (2003) Biochemistry , vol.42 , pp. 4954-4961
    • Binz, A.-K.1    Rodriguez, R.C.2    Biddison, W.E.3    Baker, B.M.4
  • 16
    • 0034641687 scopus 로고    scopus 로고
    • Assembly and dissociation of human leukocyte antigen HLA-A2 studied by real-time fluorescence resonance energy transfer
    • Gakamsky, D. M., D. M. Davis, J. L. Strominger, and I. Pecht. 2000. Assembly and dissociation of human leukocyte antigen HLA-A2 studied by real-time fluorescence resonance energy transfer. Biochemistry. 39:11163-11169.
    • (2000) Biochemistry , vol.39 , pp. 11163-11169
    • Gakamsky, D.M.1    Davis, D.M.2    Strominger, J.L.3    Pecht, I.4
  • 17
    • 0030446828 scopus 로고    scopus 로고
    • Peptide interaction with a Class I major histocompatibility complex-encoded molecule: Allosteric control of the ternary complex stability
    • Gakamsky, D. M., P. J. Bjorkman, and I. Pecht. 1996. Peptide interaction with a Class I major histocompatibility complex-encoded molecule: allosteric control of the ternary complex stability. Biochemistry. 35:14841-14848.
    • (1996) Biochemistry , vol.35 , pp. 14841-14848
    • Gakamsky, D.M.1    Bjorkman, P.J.2    Pecht, I.3
  • 20
    • 0034282919 scopus 로고    scopus 로고
    • Thermodynamic stability of HLA-B*2705-peptide complexes. Effect of peptide and major histocompatibility complex protein mutations
    • Dédier, S., S. Reinelt, T. Reitinger, G. Folkers, and D. Rognan. 2000. Thermodynamic stability of HLA-B*2705-peptide complexes. Effect of peptide and major histocompatibility complex protein mutations. J. Biol. Chem. 275:27055-27061.
    • (2000) J. Biol. Chem , vol.275 , pp. 27055-27061
    • Dédier, S.1    Reinelt, S.2    Reitinger, T.3    Folkers, G.4    Rognan, D.5
  • 21
    • 0035452568 scopus 로고    scopus 로고
    • Use of fluorescence polarization to monitor MHC-peptide interactions in solution
    • Dédier, S., S. Reinelt, S. Rion, G. Folkers, and D. Rognan. 2001. Use of fluorescence polarization to monitor MHC-peptide interactions in solution. J. Immunol. Methods. 255:57-66.
    • (2001) J. Immunol. Methods , vol.255 , pp. 57-66
    • Dédier, S.1    Reinelt, S.2    Rion, S.3    Folkers, G.4    Rognan, D.5
  • 22
    • 0035947643 scopus 로고    scopus 로고
    • Mutation of Cys-67 alters the thermodynamic stability of the human leukocyte antigen HLA-B*2705
    • Reinelt, S., S. Dédier, G. Asuni, G. Folkers, and D. Rognan. 2001. Mutation of Cys-67 alters the thermodynamic stability of the human leukocyte antigen HLA-B*2705. J. Biol. Chem. 276:18472-18477.
    • (2001) J. Biol. Chem , vol.276 , pp. 18472-18477
    • Reinelt, S.1    Dédier, S.2    Asuni, G.3    Folkers, G.4    Rognan, D.5
  • 24
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi, D. N., D. T. Hung, and D. C. Wiley. 1992. HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc. Natl. Acad. Sci. USA. 89:3429-3433.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 25
    • 0033556246 scopus 로고    scopus 로고
    • Decamer-like conformation of a non-peptide bound to HLA-B*3501 due to non-standard positioning of the C-terminus
    • Menssen, R., P. Orth, A. Ziegler, and W. Saenger. 1999. Decamer-like conformation of a non-peptide bound to HLA-B*3501 due to non-standard positioning of the C-terminus. J. Mol. Biol. 285:645-653.
    • (1999) J. Mol. Biol , vol.285 , pp. 645-653
    • Menssen, R.1    Orth, P.2    Ziegler, A.3    Saenger, W.4
  • 26
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:482-501.
    • (1994) Biophys. J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 27
    • 0037414446 scopus 로고    scopus 로고
    • Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix 8 on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study
    • Alexiev, U., I. Rimke, and T. Pöhlmann. 2003. Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix 8 on the cytoplasmic surface of bovine rhodopsin: a time-resolved fluorescence depolarization study. J. Mol. Biol. 328:705-719.
    • (2003) J. Mol. Biol , vol.328 , pp. 705-719
    • Alexiev, U.1    Rimke, I.2    Pöhlmann, T.3
  • 30
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden, D. R., J. C. Gorga, J. L. Strominger, and D. C. Wiley. 1992. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 70:1035-1048.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.