메뉴 건너뛰기




Volumn 24, Issue 6, 2003, Pages 827-835

Solution structure of a peptide derived from the β subunit of LFA-1

Author keywords

Leukocyte function associated antigen 1 (LFA 1); MIDAS domain; Peptide conformation; T cell adhesion; Turn

Indexed keywords

ARGININE; ASPARTIC ACID; CYCLOPEPTIDE; CYSTEINE; INTERCELLULAR ADHESION MOLECULE 1; LEUCINE; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; SERINE; TYROSINE;

EID: 0042430607     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(03)00170-0     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 0025195758 scopus 로고
    • Leukocyte adhesion molecules deficiency: Its structural basis, pathophysiology and implications for modulating the inflammatory response
    • Arnaout M.A. Leukocyte adhesion molecules deficiency: its structural basis, pathophysiology and implications for modulating the inflammatory response. Immunol. Rev. 114:1990;145-180.
    • (1990) Immunol. Rev. , vol.114 , pp. 145-180
    • Arnaout, M.A.1
  • 2
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 3
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax A., Davis D.G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:1985;207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 4
    • 0033135038 scopus 로고    scopus 로고
    • How LFA-1 binds to different ligands
    • Binnerts M.E., van Kooyk Y.V. How LFA-1 binds to different ligands. Immunol. Today. 20:1999;240-245.
    • (1999) Immunol. Today , vol.20 , pp. 240-245
    • Binnerts, M.E.1    Van Kooyk, Y.V.2
  • 5
    • 49349130990 scopus 로고
    • Spin-spin coupling and the conformational states of peptide systems
    • Bystrov V.F. Spin-spin coupling and the conformational states of peptide systems. Progr. NMR Spectrosc. 10:1976;41-81.
    • (1976) Progr. NMR Spectrosc. , vol.10 , pp. 41-81
    • Bystrov, V.F.1
  • 6
    • 0029608647 scopus 로고
    • Structural and dynamic properties of a β-hairpin-forming linear peptide. Modeling using ensemble-averaged constraints
    • Constantine K.L., Mueller L., Anderson N.H., Tong H., Wandler C.F., Friedrichs M.S.et al. Structural and dynamic properties of a β-hairpin-forming linear peptide. Modeling using ensemble-averaged constraints. J. Am. Chem. Soc. 117:1995;10841-10854.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10841-10854
    • Constantine, K.L.1    Mueller, L.2    Anderson, N.H.3    Tong, H.4    Wandler, C.F.5    Friedrichs, M.S.6
  • 7
    • 0007538812 scopus 로고
    • Scalar coupling constants-their analysis and their application for the elucidation of structures
    • Eberstadt M., Gemmecker G., Meirke D.F., Kessler H. Scalar coupling constants-their analysis and their application for the elucidation of structures. Angew. Chem. 107:1995;1813-1838.
    • (1995) Angew. Chem. , vol.107 , pp. 1813-1838
    • Eberstadt, M.1    Gemmecker, G.2    Meirke, D.F.3    Kessler, H.4
  • 8
  • 9
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands: Conformational, topographical and dynamic considerations
    • Hruby V.J., Al-Obeidi F., Kazmierski W. Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations. Biochem. J. 268:1990;249-262.
    • (1990) Biochem. J. , vol.268 , pp. 249-262
    • Hruby, V.J.1    Al-Obeidi, F.2    Kazmierski, W.3
  • 11
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 12
    • 0026579147 scopus 로고
    • Specific acceptance of cardiac allograft after treatment with antibodies to ICAM-1 and LFA-1
    • Isobe M., Yagita H., Okumura K., Ihara A. Specific acceptance of cardiac allograft after treatment with antibodies to ICAM-1 and LFA-1. Science. 255:1992;1125-1127.
    • (1992) Science , vol.255 , pp. 1125-1127
    • Isobe, M.1    Yagita, H.2    Okumura, K.3    Ihara, A.4
  • 13
    • 0030788925 scopus 로고    scopus 로고
    • Inhibition of homotypic adhesion of T-cells: Secondary structure of an ICAM-1 derived cyclic peptide
    • Jois S.D.S., Pal D., Tibbetts S.A., Chan M.A., Benedict S.H., Siahaan T.J. Inhibition of homotypic adhesion of T-cells: secondary structure of an ICAM-1 derived cyclic peptide. J. Peptide Res. 49:1997;517-526.
    • (1997) J. Peptide Res. , vol.49 , pp. 517-526
    • Jois, S.D.S.1    Pal, D.2    Tibbetts, S.A.3    Chan, M.A.4    Benedict, S.H.5    Siahaan, T.J.6
  • 15
    • 0033451475 scopus 로고    scopus 로고
    • Comparison of the solution conformations of a cell-adhesive peptide LBE and its reverse sequence EBL
    • Jois S.D.S., Hughes R., Siahaan T.J. Comparison of the solution conformations of a cell-adhesive peptide LBE and its reverse sequence EBL. J. Biomol. Str. Dyn. 17:1999;429-444.
    • (1999) J. Biomol. Str. Dyn. , vol.17 , pp. 429-444
    • Jois, S.D.S.1    Hughes, R.2    Siahaan, T.J.3
  • 16
    • 12644267957 scopus 로고
    • Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy
    • Kumar A., Wagner G., Ernst R.R., Wuthrich K. Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy. J. Am. Chem. Soc. 103:1981;3654-3658.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 3654-3658
    • Kumar, A.1    Wagner, G.2    Ernst, R.R.3    Wuthrich, K.4
  • 17
    • 0029287150 scopus 로고
    • Deriving accurate interproton distances from ROESY spectra with limited knowledge of scalar coupling constants via the carnival algorithm. An iterative complete-relaxation-matrix approach
    • Liu H., Banville D.L., Basus V.J., James T.L. Deriving accurate interproton distances from ROESY spectra with limited knowledge of scalar coupling constants via the carnival algorithm. An iterative complete-relaxation-matrix approach. J. Magn. Reson. 107:1995;51-59.
    • (1995) J. Magn. Reson. , vol.107 , pp. 51-59
    • Liu, H.1    Banville, D.L.2    Basus, V.J.3    James, T.L.4
  • 18
    • 0035848575 scopus 로고    scopus 로고
    • Novel p-arythio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1. Mechanism of inhibition and structure-based improvement of pharmaceutical properties
    • Liu G., Huth J.R., Olejniczak E.T., Mendoza R., DeVries P., Leitza S.et al. Novel p-arythio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1. Mechanism of inhibition and structure-based improvement of pharmaceutical properties. J. Med. Chem. 44:2001;1202-1210.
    • (2001) J. Med. Chem. , vol.44 , pp. 1202-1210
    • Liu, G.1    Huth, J.R.2    Olejniczak, E.T.3    Mendoza, R.4    DeVries, P.5    Leitza, S.6
  • 21
    • 0027068114 scopus 로고
    • Quantitative analysis of cyclic β-turn models
    • Perczel A., Fasman G.D. Quantitative analysis of cyclic β-turn models. Protein Sci. 1:1992;378-395.
    • (1992) Protein Sci. , vol.1 , pp. 378-395
    • Perczel, A.1    Fasman, G.D.2
  • 22
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel A., Park K., Fasman G.D. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide. Anal. Biochem. 203:1992;83-93.
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 26
  • 27
    • 0001812713 scopus 로고    scopus 로고
    • Counter receptor binding domains that block or enhance binding to LFA-1 or ICAM-1
    • Kaumaya PP, Hodges RS, editors. England: Mayflower Scientific
    • Siahaan TJ, Tibbetts SA, Jois SDS, Chan MA, Benedict SA. Counter receptor binding domains that block or enhance binding to LFA-1 or ICAM-1. In: Kaumaya PP, Hodges RS, editors. Peptides: chemistry, structure and biology. England: Mayflower Scientific; 1996. p. 792-3.
    • (1996) Peptides: chemistry, structure and biology , pp. 792-793
    • Siahaan, T.J.1    Tibbetts, S.A.2    Jois, S.D.S.3    Chan, M.A.4    Benedict, S.A.5
  • 29
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature. 346:1990;425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 30
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • Staunton D.E., Dustin M.L., Erickson H.P., Springer T.A. The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell. 61:1990;243-254.
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 31
    • 0024997658 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Srinivasan N., Sowdhamini R., Ramakrishnan C., Balaram P. Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Int. J. Peptide Protein Res. 36:1990;147-155.
    • (1990) Int. J. Peptide Protein Res. , vol.36 , pp. 147-155
    • Srinivasan, N.1    Sowdhamini, R.2    Ramakrishnan, C.3    Balaram, P.4
  • 32
    • 0002023923 scopus 로고
    • Structure determination from NMR data II. Computational approaches
    • Roberts GCK, editor. New York: Oxford University Press
    • Sutcliffe MJ. Structure determination from NMR data II. Computational approaches. In: Roberts GCK, editor. NMR of macromolecules: a practical Approach. New York: Oxford University Press; 1993. p. 359-90.
    • (1993) NMR of macromolecules: a practical Approach , pp. 359-390
    • Sutcliffe, M.J.1
  • 33
    • 0033568283 scopus 로고    scopus 로고
    • Peptides derived from ICAM-1 and LFA-1 modulate T-cell adhesion and immune function in a mixed lymphocyte culture
    • Tibbetts S.A., Chirathaworn C., Nakashima M., Jois S.D.S., Siahaan T.J., Chan M.A.et al. Peptides derived from ICAM-1 and LFA-1 modulate T-cell adhesion and immune function in a mixed lymphocyte culture. Transplantation. 68:1999;685-692.
    • (1999) Transplantation , vol.68 , pp. 685-692
    • Tibbetts, S.A.1    Chirathaworn, C.2    Nakashima, M.3    Jois, S.D.S.4    Siahaan, T.J.5    Chan, M.A.6
  • 34
    • 0033789773 scopus 로고    scopus 로고
    • Linear and cyclic LFA-1 and ICAM-1 peptides inhibit T cell adhesion and function
    • Tibbetts S.A., Jois S.D.S., Siahaan T.J., Benedict S.H., Chan M.A. Linear and cyclic LFA-1 and ICAM-1 peptides inhibit T cell adhesion and function. Peptides. 21:2000;1161-1167.
    • (2000) Peptides , vol.21 , pp. 1161-1167
    • Tibbetts, S.A.1    Jois, S.D.S.2    Siahaan, T.J.3    Benedict, S.H.4    Chan, M.A.5
  • 35
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T.F., Schaumann T., Gô N., Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Gô, N.5    Wüthrich, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.