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Volumn 6, Issue 5, 1998, Pages 595-604

Crystal structure of the receptor-binding domain of α2-macroglobulin

Author keywords

Crystal structure; Macroglobulins; Receptor binding domain

Indexed keywords

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0032524128     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00061-6     Document Type: Article
Times cited : (44)

References (67)
  • 1
    • 0001325160 scopus 로고
    • 2-macroglobulin and related thiol ester plasma proteins
    • (Putnam, F.W., ed.). 2nd edition, 5, Academic Press, Orlando, FL.
    • 2-macroglobulin and related thiol ester plasma proteins. In The Plasma Proteins. (Putnam, F.W., ed.). 2nd edition, 5, pp. 191-291. Academic Press, Orlando, FL.
    • (1987) The Plasma Proteins , pp. 191-291
    • Sottrup-Jensen, L.1
  • 2
    • 0024333351 scopus 로고
    • 2-macroglobulins: Structure, shape and mechanism of proteinase complex formation
    • 2-macroglobulins: structure, shape and mechanism of proteinase complex formation. J. Biol. Chem. 264, 11539-11542.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 4
    • 0015784975 scopus 로고
    • 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure
    • 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure. J. Exp. Med. 138, 508-521.
    • (1973) J. Exp. Med. , vol.138 , pp. 508-521
    • Harpel, P.C.1
  • 5
    • 0024439479 scopus 로고
    • The α-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian α-macroglobulins
    • Sottrup-Jensen, L., Sand, O., Kristensen, L. & Fey, G.H. (1989). The α-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian α-macroglobulins. J. Biol. Chem. 264, 15781-15789.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15781-15789
    • Sottrup-Jensen, L.1    Sand, O.2    Kristensen, L.3    Fey, G.H.4
  • 10
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500 kd liver membrane protein closely related to the LDL-receptor suggests a physiological role as lipoprotein receptor
    • Herz, J., Hamann, U., Rogne, S., Myklebost, O., Gausepohl, H. & Stanley, K.K. (1988). Surface location and high affinity for calcium of a 500 kd liver membrane protein closely related to the LDL-receptor suggests a physiological role as lipoprotein receptor. EMBO J. 7, 4119-4127.
    • (1988) EMBO J. , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 15
    • 0021811617 scopus 로고
    • 2-macroglobulin-trypsin complex in rat adipocytes. Evidence for different pathways
    • 2-macroglobulin-trypsin complex in rat adipocytes. Evidence for different pathways. Biochim. Biophys. Acta 845, 124-130.
    • (1985) Biochim. Biophys. Acta , vol.845 , pp. 124-130
    • Gliemann, J.1    Sonne, O.2
  • 17
    • 0023891844 scopus 로고
    • 2-macroglobulin receptor recognition site is not in the carboxyl-terminal receptor binding domain
    • 2-macroglobulin receptor recognition site is not in the carboxyl-terminal receptor binding domain. J. Biol. Chem. 263, 6715-6721.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6715-6721
    • Roche, P.A.1    Strickland, D.K.2    Enghild, J.J.3    Pizzo, S.4
  • 20
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen, W.-J., Goldstein, J.L. & Brown, M.S. (1990). NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265, 3116-3126.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3126
    • Chen, W.-J.1    Goldstein, J.L.2    Brown, M.S.3
  • 21
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
    • Daly, N.L., Scanlon, M.J., Djordjevic, J.T., Kroon, P.A. & Smith, R. (1995). Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor. Proc. Natl. Acad. Sci. USA 92, 6334-6338.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6334-6338
    • Daly, N.L.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 22
    • 0025369190 scopus 로고
    • Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment
    • Hertz, J., Kowal, R.C., Goldstein, J.L. & Brown, M.S. (1990). Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment. EMBO J. 9, 1769-1776.
    • (1990) EMBO J. , vol.9 , pp. 1769-1776
    • Hertz, J.1    Kowal, R.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 24
    • 0027376978 scopus 로고
    • 2-macroglobulin receptor containing a cluster of eight complement-type repeats
    • 2-macroglobulin receptor containing a cluster of eight complement-type repeats. J. Biol. Chem. 268, 13691-13696.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13691-13696
    • Moestrup, S.K.1    Gliemann, J.2
  • 25
    • 0027520039 scopus 로고
    • Identification of domains on the 39-kDa protein that inhibit the binding of ligands to the low density lipoprotein receptor-related protein
    • Warshawsky, I., Bu, G. & Schwartz, A.L. (1993). Identification of domains on the 39-kDa protein that inhibit the binding of ligands to the low density lipoprotein receptor-related protein. J. Biol. Chem. 268, 22046-22054.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22046-22054
    • Warshawsky, I.1    Bu, G.2    Schwartz, A.L.3
  • 28
    • 0030945761 scopus 로고    scopus 로고
    • Molecular analysis of ligand binding to the second cluster of complement-type repeats of the low density lipoprotein receptor-related protein. Evidence for an allosteric component in receptor-associated protein-mediated inhibition of ligand binding
    • Horn, I.R., Van den Berg, B.M., Van der Meijden, P.Z., Pannekoek, H. & Van Zonneveld, A.J. (1997). Molecular analysis of ligand binding to the second cluster of complement-type repeats of the low density lipoprotein receptor-related protein. Evidence for an allosteric component in receptor-associated protein-mediated inhibition of ligand binding. J. Biol. Chem. 272, 13608-13613.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13608-13613
    • Horn, I.R.1    Van Den Berg, B.M.2    Van Der Meijden, P.Z.3    Pannekoek, H.4    Van Zonneveld, A.J.5
  • 29
    • 0028101919 scopus 로고
    • Binding analysis of amino-terminal and carboxyl-terminal regions of the 39-kDa protein to the low density lipoprotein receptor-related protein
    • Warshawsky, I., Bu, G. & Schwartz, A.L. (1994). Binding analysis of amino-terminal and carboxyl-terminal regions of the 39-kDa protein to the low density lipoprotein receptor-related protein. J. Biol. Chem. 269, 3325-3330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3325-3330
    • Warshawsky, I.1    Bu, G.2    Schwartz, A.L.3
  • 30
    • 0027301838 scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds lipoprotein lipase and β-migrating very low density lipoprotein associated with the lipase
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds lipoprotein lipase and β-migrating very low density lipoprotein associated with the lipase. J. Biol. Chem. 268, 15048-15055.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15048-15055
    • Nykjær, A.1    Gliemann, J.2
  • 31
    • 0022480278 scopus 로고
    • 2-macroglobulin. Characterization of the receptor-binding domain obtained by digestion with papain
    • 2-macroglobulin. Characterization of the receptor-binding domain obtained by digestion with papain. FEBS Lett. 205, 20-24.
    • (1986) FEBS Lett. , vol.205 , pp. 20-24
    • Sottrup-Jensen, L.1    Gliemann, J.2    Van Leuven, F.3
  • 32
    • 0024583568 scopus 로고
    • A conserved region in α-macroglobulins participates in binding to the mammalian α-macroglobulin receptor
    • Enghild, J.J., Thøgersen, I.B., Roche, P.A. & Pizzo, S.V. (1989). A conserved region in α-macroglobulins participates in binding to the mammalian α-macroglobulin receptor. Biochemistry 28, 1406-1412.
    • (1989) Biochemistry , vol.28 , pp. 1406-1412
    • Enghild, J.J.1    Thøgersen, I.B.2    Roche, P.A.3    Pizzo, S.V.4
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., McArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0029933662 scopus 로고    scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein. J. Biol. Chem. 271, 12909-12912.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12909-12912
    • Nielsen, K.L.1    Thøgersen, H.C.2
  • 42
    • 0026057025 scopus 로고
    • Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP c-DNA clone by the polymerase chain reaction
    • Devrient, K., Van den Berghe, H., Cassiman, J.J. & Marynen, P. (1991). Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP c-DNA clone by the polymerase chain reaction. Biochim. Biophys. Acta 1088, 95-103.
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 95-103
    • Devrient, K.1    Van Den Berghe, H.2    Cassiman, J.J.3    Marynen, P.4
  • 43
    • 0023138170 scopus 로고
    • 2-macroglobulin and acute phase control of its messenger RNA
    • 2-macroglobulin and acute phase control of its messenger RNA. J. Biol. Chem. 262, 446-454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 446-454
    • Gehring, M.R.1    Fey, G.H.2
  • 44
    • 0026321921 scopus 로고
    • 1-macroglobulin, a broad-range proteinase inhibitor from the α-macroglobulin-complement family
    • 1-macroglobulin, a broad-range proteinase inhibitor from the α-macroglobulin-complement family. Mol. Biol. Med. 8, 287-302.
    • (1991) Mol. Biol. Med. , vol.8 , pp. 287-302
    • Eggertsen, G.1    Hudson, G.2    Shiels, B.3    Reed, D.4    Fey, G.H.5
  • 47
    • 0025861622 scopus 로고
    • 2-macroglobulin receptor (low density lipoprotein receptor-related protein)
    • 2-macroglobulin receptor (low density lipoprotein receptor-related protein). J. Biol. Chem. 266, 14011-14017.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14011-14017
    • Moestrup, S.K.1    Gliemann, J.2
  • 50
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrixes
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrixes. J. Mol. Biol. 223, 123-138.
    • (1993) J. Mol. Biol. , vol.223 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 51
    • 0026552246 scopus 로고
    • The crystal structure of diphtheria toxin
    • Choe, S., et al., & Eisenberg, D. (1992). The crystal structure of diphtheria toxin. Nature 357, 216-222.
    • (1992) Nature , vol.357 , pp. 216-222
    • Choe, S.1    Eisenberg, D.2
  • 54
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C.S., Birckbichler, P.J. & Rice, R.H. (1991). Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 5, 3071-3077.
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 55
    • 0028838976 scopus 로고
    • A low-pH reverse-phase high-performance liquid chromatography system for analysis of the phenylthiohydantoins of S-carboxymethylcysteine and S-carboxamidomethylcysteine
    • Sottrup-Jensen, L. (1995). A low-pH reverse-phase high-performance liquid chromatography system for analysis of the phenylthiohydantoins of S-carboxymethylcysteine and S-carboxamidomethylcysteine. Anal. Biochem. 225, 187-188.
    • (1995) Anal. Biochem. , vol.225 , pp. 187-188
    • Sottrup-Jensen, L.1
  • 57
    • 0002452464 scopus 로고
    • DENZO
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). DENZO. In Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 80-86. SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Data Collection and Processing , pp. 80-86
    • Otwinowski, Z.1
  • 58
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computing Project, Number 4 (1994). The CCP4 Suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 59
    • 0002700643 scopus 로고
    • Halloween... Masks and Bones
    • (Bailey, S., Hubbard, R. & Waller, D., eds), SERC Daresbury Laboratory, Warrington, UK
    • Kleywegt, G.J. & Jones, A.T. (1994). Halloween... Masks and Bones. In Proceedings of the CCP4 Study Weekend: From First Map to Final Model. (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 59-66. SERC Daresbury Laboratory, Warrington, UK.
    • (1994) Proceedings of the CCP4 Study Weekend: From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, A.T.2
  • 60
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A. Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 62
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 63
    • 52649131751 scopus 로고    scopus 로고
    • University of Göttingen, Germany
    • Sheldrick, G. (1997). SHELX-97. University of Göttingen, Germany.
    • (1997) SHELX-97
    • Sheldrick, G.1
  • 64
    • 0016430638 scopus 로고
    • Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis
    • Moews, P.C. & Kretsinger, R.H. (1975). Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis. J. Mol. Biol. 91, 201-228.
    • (1975) J. Mol. Biol. , vol.91 , pp. 201-228
    • Moews, P.C.1    Kretsinger, R.H.2
  • 65
    • 0001805131 scopus 로고
    • XABS2: An empirical absorption correction program
    • Parkin, S., Moezzi, B. & Hope, H. (1995). XABS2: an empirical absorption correction program. J. Appl. Cryst. 28, 53-56.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 53-56
    • Parkin, S.1    Moezzi, B.2    Hope, H.3
  • 66
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 67
    • 0028057108 scopus 로고
    • Raster 3D Version 2.0. A program for photorealistic molecular graphics
    • Merrit, E.A. & Murphy, M.E.P. (1994). Raster 3D Version 2.0. A program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.