Three-dimensional structure of the human plasmin α2-macroglobulin complex

Journal of Structural Biology

Volumn 123, Issue 2, 1998, Pages 124-133

  Kolodziej, Steven J ^a   Klueppelberg, H Uwe ^a,c,d   Nolasco, Norman ^a   Ehses, Wolfgang ^a,d   Strickland, Dudley K ^b   Stoops, James K ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^b HOLLAND LABORATORY   (United States)

^c Scheel Found for Cancer Research   (Germany)

^d UNIVERSITY OF COLOGNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 MACROGLOBULIN; CHYMOTRYPSIN; METHYLAMINE; PLASMA PROTEIN; PLASMIN; THIOESTER;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME ACTIVE SITE; HUMAN; KRINGLE DOMAIN; PRIORITY JOURNAL; PROTEIN STRUCTURE; THREE DIMENSIONAL IMAGING;

EID: 0031731182     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4027     Document Type: Article

References (31)

1. 2-macroglobulin with monomaleimido nanogold (Au 1.4 nm) embedded in ice, J. Struct. Biol. 109, 34-45.
2. 2-macroglobulin, J. Biol. Chem. 264, 12046-12052.
3. Chase, T., and Shaw, E. (1970) Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HCl, Methods: Companion Methods Enzymol. 19, 20-27.
4. 2-macroglobulin, Biochemistry 23, 105-111.
5. 2-macroglobulins, Electron Microsc. Rev. 5, 231-281.
6. 2-macroglobulin, J. Struct. Biol. 106, 237-242.
7. Frank, J., Radermacher, M., Penczek, P. A., Zhou, J., Li, Y., Ladjadj, M., and Leith, A. (1996) Spider and Web: Processing and visualization of images in 3D electron microscopy and related fields, J. Struct. Biol 116, 190-199.
8. Frank, J., Verschoor, A., and Wagenknecht, T. (1985) Computer processing of electron microscope images of single macromolecules, in Wu, T. T. (Ed.), New Methodologies in Studies of Protein Conformation, pp. 36-86, Van Nostrand Rhinehold, New York.
9. 2-macroglobulin-plasmin complex using monoclonal antibody-colloidal gold adducts, J. Biol. Chem. 263, 10903-10906.
10. Harpel, P. (1981) Alpha2-Plasmin inhibitor and Alpha2-macroglobulin-plasmin complexes in plasma. Quantitation by an enzyme-linked differential antibody immunosorbent assay. J. Clin. Invest. 68, 46-55.
11. Hessler, D., Young, S. J., Carragher, B., Martone, M., Hinshaw, J., Milligan, R., Masliah, E., Whittaker, M., Lamont, S., and Ellisman, M. (1992) SYNU: Software for visualization of 3-dimensional biological structure, in Lyman, C. E., Peachey L. D., and Fisher, R. M. (Eds.), Microscopy: The Key Research Tool, pp. 73-82, EMSA, Milwaukee.
12. Kolodziej, S. J., Penczek, P. A., and Stoops, J. K. (1997) Utility of butvar support film and methylamine tungstate stain in three-dimensional electron microscopy: Agreement between stain and frozen-hydrated reconstructions, J. Struct. Biol. 120, 158-167.
13. Morris, J. P., Blatt, S., Powell, J., Strickland, D. K., and Castellino, F. J. (1981) Role of lysine binding regions in the kinetic properties of human plasmin, Biochemistry 20, 4811-4816.
14. Oliver, R. M. (1973) Negative stain electron microscopy of protein macromolecules, Methods: Companion Methods Enzymol. 27, 616-672.
15. Penczek, P. A., Grassucci, R. A., and Frank, J. (1994) The ribosome at improved resolution: new techniques for merging and orientation refinement in 3-D cryo-electron microscopy of biological particles, Ultramicroscopy 53, 251-270.
16. Penczek, P., Radermacher, M., and Frank, J. (1992) Three-dimensional reconstruction of single particles embedded in ice, Ultramicroscopy 40, 33-53.
17. 2-macroglobulin upon proteinase entrapment: Three-dimensional structure of the half-transformed molecule, J. Biol. Chem. 273, 8987-8993.
18. Radermacher, M. (1988) Three-dimensional reconstruction of single particles from random and non-random tilt series, J. Electron Microsc. Technol. 9, 359-394.
19. Ramakrishnan, V., Patthy, L., and Mangel, W. F. (1991) Conformation of lys-plasminogen and the kringle 1-3 fragment of plasminogen analyzed by small-angle neutron scattering. Biochemistry 30, 3963-3969.
20. Roche, P. A., and Pizzo, S. V. (1987) The role of histidyl residues in zinc-induced precipitation of alpha 2-macroglobulin-proteinase complexes. Biochemistry 26, 486-491.
21. Saxton, W. O., and Baumeister, W. (1982) The correlation averaging of a regularly arranged bacterial cell envelope protein, J. Microsc. 127, 127-138.
22. Schroeter, J. P., and Bretaudiere, J.-P. (1996) SUPRIM: Easily modified image processing software, J. Struct. Biol. 116, 131-137.
23. 2-macroglobulin-methylamine and chymotrypsin complexes, J. Struct. Biol. 109, 235-247.
24. 2-Macroglobulins: Structure, shape, and mechanisms of protein complex formation, J. Biol. Chem. 264, 11539-11542
25. 2-Macroglobulin, a physiological regulator of proteinase activity, in Barrett, A. J. (Ed.) Proteinases in Mammalian Cells and Tissues, pp. 663-696, Elsevier-North Holland, Amsterdam.
26. 2-macroglobulin: Evidence for two functional domains, Biochemistry 24, 2993-3001.
27. 2-macroglobulin: Effect of antifibrinolytic agents, Biochemistry 26, 8487-8495.
28. Stoops, J. K., Baker, T. S., Schroeter, J. P., Kolodziej, S. J., Niu, X.-D., and Reed, L. J. (1992) Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images, J. Biol. Chem. 267, 24769-24775.
29. Stoops, J. K., Momany, C., Oliver, R. M., Schroeter, J. P., Bretaudiere, J.-P., and Hackert, M. L. (1991) Comparisons of the low-resolution structures of ornithine decarboxylase by electron microscopy and x-ray crystallography: The utility of methylamine tungstate and Butvar support film in the study of macromolecules by transmission electron microscopy, J. Electron Microsc. Technol. 18, 157-166.
30. Unser, M., Trus, B. L., and Stevens, A. C. (1987) A new resolution criterion based on spectral signal-to-noise ratios, Ultramicroscopy 23, 39-51.
31. Vlaicu, R., Rus, H. G., Niculescu, F., and Cristae, A. (1985) Immunoglobulins and complement components in human aortic atherosclerosis intima, Atherosclerosis 55, 35-50.