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Volumn 335, Issue 4, 2004, Pages 1019-1028

Structure of the Integrin α2β1-binding Collagen Peptide

Author keywords

Collagen; Integrin binding; Triple helix

Indexed keywords

AMINO ACID DERIVATIVE; ARGININE; COLLAGEN; GLUTAMIC ACID; HEXAPEPTIDE; PEPTIDE; VERY LATE ACTIVATION ANTIGEN 2; WATER;

EID: 0347123535     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.030     Document Type: Article
Times cited : (119)

References (28)
  • 1
    • 0030963588 scopus 로고    scopus 로고
    • The collagen triple-helix structure
    • Brodsky B., Ramshaw J.A.M. The collagen triple-helix structure. Matrix Biol. 15:1997;545-554.
    • (1997) Matrix Biol. , vol.15 , pp. 545-554
    • Brodsky, B.1    Ramshaw, J.A.M.2
  • 3
    • 0025319808 scopus 로고
    • Energetics of intrachain salt linkage formation in collagen
    • Katz E.P., David C.W. Energetics of intrachain salt linkage formation in collagen. Biopolymers. 29:1990;791-798.
    • (1990) Biopolymers , vol.29 , pp. 791-798
    • Katz, E.P.1    David, C.W.2
  • 4
    • 0027053121 scopus 로고
    • Unique side-chain conformation encoding for chirality and azimuthal orientation in the molecular packing of skin collagen
    • Katz E.P., David C.W. Unique side-chain conformation encoding for chirality and azimuthal orientation in the molecular packing of skin collagen. J. Mol. Biol. 228:1992;963-969.
    • (1992) J. Mol. Biol. , vol.228 , pp. 963-969
    • Katz, E.P.1    David, C.W.2
  • 5
    • 0032563109 scopus 로고    scopus 로고
    • X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)
    • Kramer R.Z., Vitagliano L., Bella J., Berisio R., Mazzarella L., Brodsky B. X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly). J. Mol. Biol. 280:1998;623-638.
    • (1998) J. Mol. Biol. , vol.280 , pp. 623-638
    • Kramer, R.Z.1    Vitagliano, L.2    Bella, J.3    Berisio, R.4    Mazzarella, L.5    Brodsky, B.6
  • 6
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer R.Z., Bella J., Mayville P., Brodsky B., Berman H.M. Sequence dependent conformational variations of collagen triple-helical structure. Nature Struct. Biol. 6:1999;454-457.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 7
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella J., Eaton M., Brodsky B., Berman H.M. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science. 266:1994;75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 8
    • 0034283338 scopus 로고    scopus 로고
    • Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair
    • Kramer R.Z., Venugopal M.G., Bella J., Mayville P., Brodsky B., Berman H.M. Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair. J. Mol. Biol. 301:2000;1191-1205.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1191-1205
    • Kramer, R.Z.1    Venugopal, M.G.2    Bella, J.3    Mayville, P.4    Brodsky, B.5    Berman, H.M.6
  • 9
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family-structures, functions and their role on leukocytes
    • Hemler M.E. VLA proteins in the integrin family-structures, functions and their role on leukocytes. Annu. Rev. Immunol. 8:1990;365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 10
    • 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
  • 13
    • 0034283814 scopus 로고    scopus 로고
    • Integrin and ECM functions: Roles in vertebrate development
    • De Arcangelis A., Georges-Labouesse E. Integrin and ECM functions: roles in vertebrate development. Trends Genet. 16:2000;389-395.
    • (2000) Trends Genet. , vol.16 , pp. 389-395
    • De Arcangelis, A.1    Georges-Labouesse, E.2
  • 14
    • 0032509342 scopus 로고    scopus 로고
    • Identification in collagen type I of an integrin α2β1-binding site containing an essential GER sequence
    • Knight C.G., Morton L.F., Onley D.J., Peachey A.R., Messent A.J., Smethurst P.A., et al. Identification in collagen type I of an integrin α2β1-binding site containing an essential GER sequence. J. Biol. Chem. 273:1998;33287-33294.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33287-33294
    • Knight, C.G.1    Morton, L.F.2    Onley, D.J.3    Peachey, A.R.4    Messent, A.J.5    Smethurst, P.A.6
  • 15
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight C.G., Morton L.F., Peachey A.R., Tuckwell D.S., Farndale R.W., Barnes M.J. The collagen-binding A-domains of integrins α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J. Biol. Chem. 275:2000;35-40.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 17
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence
    • Kramer R.Z., Bella J., Brodsky B., Berman H.M. The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J. Mol. Biol. 311:2001;131-147.
    • (2001) J. Mol. Biol. , vol.311 , pp. 131-147
    • Kramer, R.Z.1    Bella, J.2    Brodsky, B.3    Berman, H.M.4
  • 18
    • 0034141727 scopus 로고    scopus 로고
    • Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases
    • Ottl J., Gabriel D., Murphy G., Knäuper V., Tominaga Y., Nagase H., et al. Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases. Chem. Biol. 7:2000;119.
    • (2000) Chem. Biol. , vol.7 , pp. 119
    • Ottl, J.1    Gabriel, D.2    Murphy, G.3    Knäuper, V.4    Tominaga, Y.5    Nagase, H.6
  • 19
    • 0036298978 scopus 로고    scopus 로고
    • Peptide investigations of pairwise interactions in the collagen triple-helix
    • Persikov A.V., Ramshaw J.A., Kirkpatrick A., Brodsky B. Peptide investigations of pairwise interactions in the collagen triple-helix. J. Mol. Biol. 316:2002;385-394.
    • (2002) J. Mol. Biol. , vol.316 , pp. 385-394
    • Persikov, A.V.1    Ramshaw, J.A.2    Kirkpatrick, A.3    Brodsky, B.4
  • 20
    • 0025618549 scopus 로고
    • The collagen fibril - A model system for studying the staining and fixation of a protein
    • Chapman J.A., Tzaphlidou M., Meek K.M., Kadler K.E. The collagen fibril - a model system for studying the staining and fixation of a protein. Electron Microsc. Rev. 3:1990;143-182.
    • (1990) Electron Microsc. Rev. , vol.3 , pp. 143-182
    • Chapman, J.A.1    Tzaphlidou, M.2    Meek, K.M.3    Kadler, K.E.4
  • 22
    • 0036438891 scopus 로고    scopus 로고
    • The chain register in heterotrimeric collagen peptides affects triple helix stability and folding kinetics
    • Sacca B., Renner C., Mororder L. The chain register in heterotrimeric collagen peptides affects triple helix stability and folding kinetics. J. Mol. Biol. 324:2002;309-318.
    • (2002) J. Mol. Biol. , vol.324 , pp. 309-318
    • Sacca, B.1    Renner, C.2    Mororder, L.3
  • 23
    • 0033541429 scopus 로고    scopus 로고
    • Cell surface receptors transmit sufficient force to bend collagen fibrils
    • Lee G.M., Loeser R.F. Cell surface receptors transmit sufficient force to bend collagen fibrils. Expt. Cell Res. 248:1999;294.
    • (1999) Expt. Cell Res. , vol.248 , pp. 294
    • Lee, G.M.1    Loeser, R.F.2
  • 24
    • 84920325457 scopus 로고
    • AMoRe: An automated molecular replacement package
    • Navaza J. AMoRe: an automated molecular replacement package. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.