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Volumn 109, Issue 14, 2012, Pages 5253-5258

Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex

Author keywords

Extracellular matrix; X ray crystallography

Indexed keywords

COLLAGEN TYPE 1; VON WILLEBRAND FACTOR;

EID: 84859467505     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1112388109     Document Type: Article
Times cited : (69)

References (47)
  • 1
    • 0034783234 scopus 로고    scopus 로고
    • The molecular biology of von willebrand disease
    • DOI 10.1046/j.1365-2257.2001.00400.x
    • Keeney S, Cumming AM (2001) The molecular biology of von Willebrand disease. Clin Lab Haematol 23:209-230. (Pubitemid 32995166)
    • (2001) Clinical and Laboratory Haematology , vol.23 , Issue.4 , pp. 209-230
    • Keeney, S.1    Cumming, A.M.2
  • 2
    • 0030770612 scopus 로고    scopus 로고
    • The von Willebrand factor A3 domain does not contain a metal ion- dependent adhesion site motif
    • DOI 10.1074/jbc.272.40.25162
    • Bienkowska J, Cruz M, Atiemo A, Handin R, Liddington R (1997) The von Willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J Biol Chem 272:25162-25167. (Pubitemid 27415701)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25162-25167
    • Bienkowska, J.1    Cruz, M.2    Atiemo, A.3    Handin, R.4    Liddington, R.5
  • 3
    • 0031571750 scopus 로고    scopus 로고
    • Crystal structure of the A3 domain of human von Willebrand factor: Implications for collagen binding
    • Huizinga EG, Van der Plas M, Kroon J, Sixma JJ, Gros P (1997) Crystal structure of the A3 domain of human von Willebrand factor: Implications for collagen binding. Structure 5:1147-1156.
    • (1997) Structure , vol.5 , pp. 1147-1156
    • Huizinga, E.G.1    Van Der Plas, M.2    Kroon, J.3    Sixma, J.J.4    Gros, P.5
  • 4
    • 67249086879 scopus 로고    scopus 로고
    • Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor
    • Zhang Q, et al. (2009) Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci USA 106:9226-9231.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9226-9231
    • Zhang, Q.1
  • 6
    • 0035971244 scopus 로고    scopus 로고
    • Identification of the collagen-binding site of the von Willebrand factor A3-domain
    • Romijn RA, et al. (2001) Identification of the collagen-binding site of the von Willebrand factor A3-domain. J Biol Chem 276:9985-9991.
    • (2001) J Biol Chem , vol.276 , pp. 9985-9991
    • Romijn, R.A.1
  • 8
    • 33845268866 scopus 로고    scopus 로고
    • A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides
    • DOI 10.1182/blood-2006-03-011965
    • Lisman T, et al. (2006) A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides. Blood 108:3753-3756. (Pubitemid 44864555)
    • (2006) Blood , vol.108 , Issue.12 , pp. 3753-3756
    • Lisman, T.1    Raynal, N.2    Groeneveld, D.3    Maddox, B.4    Peachey, A.R.5    Huizinga, E.G.6    De Groot, P.G.7    Farndale, R.W.8
  • 9
    • 50349096759 scopus 로고    scopus 로고
    • Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens
    • Giudici C, et al. (2008) Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens. J Biol Chem 283:19551-19560.
    • (2008) J Biol Chem , vol.283 , pp. 19551-19560
    • Giudici, C.1
  • 10
    • 42449119742 scopus 로고    scopus 로고
    • Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen
    • Konitsiotis AD, et al. (2008) Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen. J Biol Chem 283:6861-6868.
    • (2008) J Biol Chem , vol.283 , pp. 6861-6868
    • Konitsiotis, A.D.1
  • 11
    • 78951473449 scopus 로고    scopus 로고
    • Collagen binding specificity of the discoidin domain receptors: Binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1
    • Xu H, et al. (2011) Collagen binding specificity of the discoidin domain receptors: Binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol 30:16-26.
    • (2011) Matrix Biol , vol.30 , pp. 16-26
    • Xu, H.1
  • 15
    • 70350722434 scopus 로고    scopus 로고
    • Characterization of W1745C and S1783A: Two novel mutations causing defective collagen binding in the A3 domain of von Willebrand factor
    • Riddell AF, et al. (2009) Characterization of W1745C and S1783A: Two novel mutations causing defective collagen binding in the A3 domain of von Willebrand factor. Blood 114:3489-3496.
    • (2009) Blood , vol.114 , pp. 3489-3496
    • Riddell, A.F.1
  • 18
    • 71049118163 scopus 로고    scopus 로고
    • Crystallographic insight into collagen recognition by discoidin domain receptor 2
    • Carafoli F, et al. (2009) Crystallographic insight into collagen recognition by discoidin domain receptor 2. Structure 17:1573-1581.
    • (2009) Structure , vol.17 , pp. 1573-1581
    • Carafoli, F.1
  • 19
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella J, Brodsky B, Berman HM (1995) Hydration structure of a collagen peptide. Structure 3:893-906.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 20
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular, structure of a collagen-like peptide with a biologically relevant sequence
    • DOI 10.1006/jmbi.2001.4849
    • Kramer RZ, Bella J, Brodsky B, Berman HM (2001) The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J Mol Biol 311:131-147. (Pubitemid 32735320)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 131-147
    • Kramer, R.Z.1    Bella, J.2    Brodsky, B.3    Berman, H.M.4
  • 22
    • 0034671734 scopus 로고    scopus 로고
    • Multiple binding sites in collagen type I for the integrins α1β1 and α2β1
    • Xu Y, et al. (2000) Multiple binding sites in collagen type I for the integrins α1β1 and α2β1. J Biol Chem 275:38981-38989.
    • (2000) J Biol Chem , vol.275 , pp. 38981-38989
    • Xu, Y.1
  • 23
    • 25444479366 scopus 로고    scopus 로고
    • A novel binding site in collagen type III for integrins α1β1 and α2β1
    • Kim JK, et al. (2005) A novel binding site in collagen type III for integrins α1β1 and α2β1. J Biol Chem 280:32512-32520.
    • (2005) J Biol Chem , vol.280 , pp. 32512-32520
    • Kim, J.K.1
  • 25
    • 0017852314 scopus 로고
    • Sequence regularities and packing of collagen molecules
    • Piez KA, Trus BL (1978) Sequence regularities and packing of collagen molecules. J Mol Biol 122:419-432. (Pubitemid 8401315)
    • (1978) Journal of Molecular Biology , vol.122 , Issue.4 , pp. 419-432
    • Piez, K.A.1    Trus, B.L.2
  • 26
    • 0020417308 scopus 로고
    • Type I collagen segment long spacing banding patterns. Evidence that the alpha2 chain is in the reference or a position
    • Bender E, Silver FH, Hayashi K, Trelstad RL (1982) Type I collagen segment long spacing banding patterns. Evidence that the alpha2 chain is in the reference or A position. J Biol Chem 257:9653-9657. (Pubitemid 13205129)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.16 , pp. 9653-9657
    • Bender, E.1    Silver, F.H.2    Hayashi, K.3    Trelstad, R.L.4
  • 27
    • 0017103671 scopus 로고
    • Contribution of the alpha2 chain to the molecular stability of collagen
    • Traub W, Fietzek PP (1976) Contribution of the alpha2 chain to the molecular stability of collagen. FEBS Lett 68:245-249.
    • (1976) FEBS Lett , vol.68 , pp. 245-249
    • Traub, W.1    Fietzek, P.P.2
  • 28
    • 0018068793 scopus 로고
    • The role of polar and hydrophobic interactions for the molecular packing of type I collagen: A three-dimensional evaluation of the amino acid sequence
    • Hofmann H, Fietzek PP, Kuhn K (1978) The role of polar and hydrophobic interactions for the molecular packing of type I collagen: A three-dimensional evaluation of the amino acid sequence. J Mol Biol 125:137-165. (Pubitemid 9052128)
    • (1978) Journal of Molecular Biology , vol.125 , Issue.2 , pp. 137-165
    • Hofmann, H.1    Fietzek, P.P.2    Kuhn, K.3
  • 31
    • 34547575826 scopus 로고    scopus 로고
    • SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts
    • DOI 10.1074/jbc.M700167200
    • Rentz TJ, Poobalarahi F, Bornstein P, Sage EH, Bradshaw AD (2007) SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts. J Biol Chem 282:22062-22071. (Pubitemid 47195756)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 22062-22071
    • Rentz, T.J.1    Poobalarahi, F.2    Bornstein, P.3    Sage, E.H.4    Bradshaw, A.D.5
  • 33
    • 0021079184 scopus 로고
    • The interaction between collagens and factor VIII/Von Willebrand factor: Investigation of the structural requirements for interaction
    • Morton LF, Griffin B, Pepper DS, Barnes MJ (1983) The interaction between collagens and factor VIII/von Willebrand factor: Investigation of the structural requirements for interaction. Thromb Res 32:545-556. (Pubitemid 14216152)
    • (1983) Thrombosis Research , vol.32 , Issue.6 , pp. 545-556
    • Morton, L.F.1    Griffin, B.2    Pepper, D.S.3    Barnes, M.J.4
  • 34
    • 67749124481 scopus 로고    scopus 로고
    • Structural insights into the interactions between platelet receptors and fibrillar collagen
    • Herr AB, Farndale RW (2009) Structural insights into the interactions between platelet receptors and fibrillar collagen. J Biol Chem 284:19781-19785.
    • (2009) J Biol Chem , vol.284 , pp. 19781-19785
    • Herr, A.B.1    Farndale, R.W.2
  • 35
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • Hulmes DJ, Wess TJ, Prockop DJ, Fratzl P (1995) Radial packing, order, and disorder in collagen fibrils. Biophys J 68:1661-1670.
    • (1995) Biophys J , vol.68 , pp. 1661-1670
    • Hulmes, D.J.1    Wess, T.J.2    Prockop, D.J.3    Fratzl, P.4
  • 37
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran GN, Kartha G (1955) Structure of collagen. Nature 176:593-595.
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 38
    • 32844463093 scopus 로고
    • The structure of collagen
    • Rich A, Crick FH (1955) The structure of collagen. Nature 176:915-916.
    • (1955) Nature , vol.176 , pp. 915-916
    • Rich, A.1    Crick, F.H.2
  • 39
    • 69949138651 scopus 로고    scopus 로고
    • Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc Natl Acad Sci USA, 103, 9001-9005
    • lett
    • Okuyama K, et al. (2009) Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc Natl Acad Sci USA, 103, 9001-9005. Acta Crystallogr D Biol Crystallogr 65:1007-1008 (lett).
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 1007-1008
    • Okuyama, K.1
  • 41
    • 0037093219 scopus 로고    scopus 로고
    • Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons
    • DOI 10.1182/blood.V99.10.3623
    • Wu D, et al. (2002) Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons. Blood 99:3623-3628. (Pubitemid 34534531)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3623-3628
    • Wu, D.1    Vanhoorelbeke, K.2    Cauwenberghs, N.3    Meiring, M.4    Depraetere, H.5    Kotze, H.F.6    Deckmyn, H.7
  • 42
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 45
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the crystallography and NMR system. Nat Protoc 2:2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


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