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Volumn 186, Issue 1, 2014, Pages 75-85

Structural diversity of a collagen-binding matrix protein from the byssus of blue mussels upon refolding

Author keywords

Disulfide isomers; Proximal thread matrix protein 1 (PTMP1); Refolding; Structural stability; VWA domains

Indexed keywords

COLLAGEN BINDING PROTEIN; ISOPROTEIN; MATRIX PROTEIN; MONOMER; PROTEIN PTMP1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; SCLEROPROTEIN;

EID: 84898597786     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2014.02.013     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0017378513 scopus 로고
    • Formation of the four isomers of hen egg white lysozyme containing three native disulfide bonds and one open disulfide bond
    • Acharya A.S., Taniuchi H. Formation of the four isomers of hen egg white lysozyme containing three native disulfide bonds and one open disulfide bond. Proc. Natl. Acad. Sci. U S A 1977, 74:2362-2366.
    • (1977) Proc. Natl. Acad. Sci. U S A , vol.74 , pp. 2362-2366
    • Acharya, A.S.1    Taniuchi, H.2
  • 2
    • 33846592202 scopus 로고    scopus 로고
    • Conformational stability and domain unfolding of the von Willebrand factor A domains
    • Auton M., Cruz M.A., Moake J. Conformational stability and domain unfolding of the von Willebrand factor A domains. J. Mol. Biol. 2007, 366:986-1000.
    • (2007) J. Mol. Biol. , vol.366 , pp. 986-1000
    • Auton, M.1    Cruz, M.A.2    Moake, J.3
  • 3
    • 0017231408 scopus 로고
    • The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. IV. Observations by transmission electron microscopy
    • Bairati A., Vitellaro-Zuccarello L. The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. IV. Observations by transmission electron microscopy. Cell Tissue Res. 1976, 166:219-234.
    • (1976) Cell Tissue Res. , vol.166 , pp. 219-234
    • Bairati, A.1    Vitellaro-Zuccarello, L.2
  • 5
    • 0000508581 scopus 로고    scopus 로고
    • Mechanical design of mussel byssus: material yield enhances attachment strength
    • Bell E., Gosline J. Mechanical design of mussel byssus: material yield enhances attachment strength. J. Exp. Biol. 1996, 199:1005-1017.
    • (1996) J. Exp. Biol. , vol.199 , pp. 1005-1017
    • Bell, E.1    Gosline, J.2
  • 6
    • 84859467505 scopus 로고    scopus 로고
    • Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex
    • Brondijk T.H.C., Bihan D., Farndale R.W., Huizinga E.G. Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex. Proc. Natl. Acad. Sci. USA 2012, 109:5253-5258.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5253-5258
    • Brondijk, T.H.C.1    Bihan, D.2    Farndale, R.W.3    Huizinga, E.G.4
  • 7
    • 0001201662 scopus 로고
    • Some structural proteins of Mytilus edulis
    • Brown C.H. Some structural proteins of Mytilus edulis. Q. J. Microsc. Sci. 1952, 93:487-502.
    • (1952) Q. J. Microsc. Sci. , vol.93 , pp. 487-502
    • Brown, C.H.1
  • 9
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 10
    • 0028914676 scopus 로고
    • Interaction of the von Willebrand factor (vWF) with collagen
    • Cruz M.A., Yuan H., Lee J.R., Wise R.J., Handin R.I. Interaction of the von Willebrand factor (vWF) with collagen. J. Biol. Chem. 1995, 270:10822-10827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10822-10827
    • Cruz, M.A.1    Yuan, H.2    Lee, J.R.3    Wise, R.J.4    Handin, R.I.5
  • 11
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A., Huang P., Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990, 29:3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 13
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib
    • Emsley J., Cruz M., Handin R., Liddington R. Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib. J. Biol. Chem. 1998, 273:10396-10401.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Handin, R.3    Liddington, R.4
  • 15
    • 36849090781 scopus 로고    scopus 로고
    • Structural and functional characterization of recombinant matrilin-3 a-domain and implications for human genetic bone diseases
    • Fresquet M., Jowitt T.A., Ylöstalo J., Coffey P., Meadows R.S., Ala-Kokko L., Thornton D.J., Briggs M.D. Structural and functional characterization of recombinant matrilin-3 a-domain and implications for human genetic bone diseases. J. Biol. Chem. 2007, 282:34634-34643.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34634-34643
    • Fresquet, M.1    Jowitt, T.A.2    Ylöstalo, J.3    Coffey, P.4    Meadows, R.S.5    Ala-Kokko, L.6    Thornton, D.J.7    Briggs, M.D.8
  • 17
    • 79960925340 scopus 로고    scopus 로고
    • Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads
    • Hagenau A., Papadopoulos P., Kremer F., Scheibel T. Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads. J. Struct. Biol. 2011, 175:339-347.
    • (2011) J. Struct. Biol. , vol.175 , pp. 339-347
    • Hagenau, A.1    Papadopoulos, P.2    Kremer, F.3    Scheibel, T.4
  • 18
    • 66149108464 scopus 로고    scopus 로고
    • Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis
    • Hagenau A., Scheidt H.A., Serpell L., Huster D., Scheibel T. Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis. Macromol. Biosci. 2009, 9:162-168.
    • (2009) Macromol. Biosci. , vol.9 , pp. 162-168
    • Hagenau, A.1    Scheidt, H.A.2    Serpell, L.3    Huster, D.4    Scheibel, T.5
  • 19
    • 44449158136 scopus 로고    scopus 로고
    • PH-dependent locking of giant mesogens in fibers drawn from mussel byssal collagens
    • Harrington M.J., Waite J.H. PH-dependent locking of giant mesogens in fibers drawn from mussel byssal collagens. Biomacromolecules 2008, 9:1480-1486.
    • (2008) Biomacromolecules , vol.9 , pp. 1480-1486
    • Harrington, M.J.1    Waite, J.H.2
  • 22
    • 0031571750 scopus 로고    scopus 로고
    • Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding
    • Huizinga E.G., van der Plas R.M., Kroon J., Sixma J.J., Gros P. Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding. Structure 1997, 5:1147-1156.
    • (1997) Structure , vol.5 , pp. 1147-1156
    • Huizinga, E.G.1    van der Plas, R.M.2    Kroon, J.3    Sixma, J.J.4    Gros, P.5
  • 23
    • 0014409423 scopus 로고
    • The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content
    • Janatova J., Fuller J.K., Hunter M.J. The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content. J. Biol. Chem. 1968, 243:3612-3622.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3612-3622
    • Janatova, J.1    Fuller, J.K.2    Hunter, M.J.3
  • 24
    • 0019599157 scopus 로고
    • Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
    • Kauppinen J.K., Moffatt D.J., Mantsch H.H., Cameron D.G. Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours. Anal. Chem. 1981, 53:1454-1457.
    • (1981) Anal. Chem. , vol.53 , pp. 1454-1457
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 26
    • 2342454381 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor
    • Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., Collier R.J. Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. Proc. Natl. Acad. Sci. USA 2004, 101:6367-6372.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6367-6372
    • Lacy, D.B.1    Wigelsworth, D.J.2    Scobie, H.M.3    Young, J.A.T.4    Collier, R.J.5
  • 27
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18)
    • Lee J.-O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18). Cell 1995, 80:631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 28
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman I., Fuchs R., Helenius A. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 1986, 55:663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 30
    • 84866373857 scopus 로고    scopus 로고
    • MMass as a software tool for the annotation of cyclic peptide tandem mass spectra
    • Niedermeyer T.H.J., Strohalm M. mMass as a software tool for the annotation of cyclic peptide tandem mass spectra. PLoS One 2012, 7:e44913.
    • (2012) PLoS One , vol.7
    • Niedermeyer, T.H.J.1    Strohalm, M.2
  • 31
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Pace C.N., Shaw K.L. Linear extrapolation method of analyzing solvent denaturation curves. Proteins Struct. Funct. Bioinformat. 2000, 41:1-7.
    • (2000) Proteins Struct. Funct. Bioinformat. , vol.41 , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 32
    • 0029267044 scopus 로고
    • Exotic collagen gradients in the byssus of the mussel Mytilus edulis
    • Qin X., Waite J.H. Exotic collagen gradients in the byssus of the mussel Mytilus edulis. J. Exp. Biol. 1995, 198:633-644.
    • (1995) J. Exp. Biol. , vol.198 , pp. 633-644
    • Qin, X.1    Waite, J.H.2
  • 33
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin
    • Qu A., Leahy D.J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc. Natl. Acad. Sci. USA 1995, 92:10277-10281.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 36
    • 67650046983 scopus 로고    scopus 로고
    • Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis
    • Sagert J., Waite J.H. Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis. J. Exp. Biol. 2009, 212:2224-2236.
    • (2009) J. Exp. Biol. , vol.212 , pp. 2224-2236
    • Sagert, J.1    Waite, J.H.2
  • 37
    • 33751571086 scopus 로고    scopus 로고
    • Smith, A.M., Callow, J.A., (Eds.), Biological Adhesives, Springer-Verlag, Berlin, Heidelberger Platz 3, D-14197 Berlin, Germany
    • Sagert, J., Sun, C., Waite, J.H. 2006. Chemical subtleties of mussel and polychaete holdfasts. In: Smith, A.M., Callow, J.A., (Eds.), Biological Adhesives, Springer-Verlag, Berlin, Heidelberger Platz 3, D-14197 Berlin, Germany, pp. 125-143.
    • (2006) Chemical subtleties of mussel and polychaete holdfasts , pp. 125-143
    • Sagert, J.1    Sun, C.2    Waite, J.H.3
  • 38
    • 33745931632 scopus 로고    scopus 로고
    • A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli
    • Schlapschy M., Grimm S., Skerra A. A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli. Protein Eng. Des. Sel. 2006, 19:385-390.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 385-390
    • Schlapschy, M.1    Grimm, S.2    Skerra, A.3
  • 39
    • 84905506446 scopus 로고    scopus 로고
    • 2014a. Crystallization and preliminary X-ray diffraction analysis of Proximal Thread Matrix Protein 1 (PTMP1) from Mytilus galloprovincialis. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. manuscript submitted.
    • Suhre, M.H., Scheibel, T., Steegborn, C., Gertz, M., 2014a. Crystallization and preliminary X-ray diffraction analysis of Proximal Thread Matrix Protein 1 (PTMP1) from Mytilus galloprovincialis. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. manuscript submitted.
    • Suhre, M.H.1    Scheibel, T.2    Steegborn, C.3    Gertz, M.4
  • 40
    • 84905506858 scopus 로고    scopus 로고
    • Structural and functional features of a collagen binding matrix protein from the mussel byssus
    • Suhre M.H., Gertz M., Steegborn C., Scheibel T. Structural and functional features of a collagen binding matrix protein from the mussel byssus. Nat. Commun 2014, 10.1038/ncomms4392.
    • (2014) Nat. Commun
    • Suhre, M.H.1    Gertz, M.2    Steegborn, C.3    Scheibel, T.4
  • 41
    • 0035193168 scopus 로고    scopus 로고
    • Oxidative stress and the mechanical properties of naturally occurring chimeric collagen-containing fibers
    • Sun C., Vaccaro E., Waite J.H. Oxidative stress and the mechanical properties of naturally occurring chimeric collagen-containing fibers. Biophys. J. 2001, 81:3590-3595.
    • (2001) Biophys. J. , vol.81 , pp. 3590-3595
    • Sun, C.1    Vaccaro, E.2    Waite, J.H.3
  • 42
    • 0036856907 scopus 로고    scopus 로고
    • Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers
    • Sun C., Lucas J.M., Waite J.H. Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers. Biomacromolecules 2002, 3:1240-1248.
    • (2002) Biomacromolecules , vol.3 , pp. 1240-1248
    • Sun, C.1    Lucas, J.M.2    Waite, J.H.3
  • 45
    • 2942707997 scopus 로고    scopus 로고
    • Exploring molecular and mechanical gradients in structural bioscaffolds
    • Waite J.H., Lichtenegger H.C., Stucky G.D., Hansma P. Exploring molecular and mechanical gradients in structural bioscaffolds. Biochemistry 2004, 43:7653-7662.
    • (2004) Biochemistry , vol.43 , pp. 7653-7662
    • Waite, J.H.1    Lichtenegger, H.C.2    Stucky, G.D.3    Hansma, P.4
  • 46
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin a domains: widely dispersed adhesion and elsewhere
    • Whittaker C.A., Hynes R.O. Distribution and evolution of von Willebrand/integrin a domains: widely dispersed adhesion and elsewhere. Mol. Biol. Cell 2002, 13:3369-3387.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 48
    • 5844368173 scopus 로고
    • The scattering of light and the radial distribution function of high polymer solutions
    • Zimm B.H. The scattering of light and the radial distribution function of high polymer solutions. J. Chem. Phys. 1948, 16:1093-1099.
    • (1948) J. Chem. Phys. , vol.16 , pp. 1093-1099
    • Zimm, B.H.1


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