Related Content
Search Google Scholar for:
|
|
Science 6 April 1990:
Vol. 248. no. 4951, pp. 69 - 73
DOI: 10.1126/science.2108500
|
|
Articles
Science, Vol 248, Issue 4951, 69-73
Copyright © 1990 by American Association for the Advancement of Science
Characterization of an extremely large, ligand-induced conformational change in plasminogen
WF Mangel,
BH Lin,
and
V Ramakrishnan
Biology Department, Brookhaven National Laboratory, Upton, NY 11973.
Native human plasminogen has a radius of gyration of 39 angstroms. Upon occupation of a weak lysine binding site, the radius of gyration increases to 56 angstroms, an extremely large ligand-induced conformational change. There are no intermediate conformational states between the closed and open form. The conformational chang is not accompanied by a change in secondary structure, hence the closed conformation is formed by interaction between domains that is abolished upon conversion to the open form. This reversible change in conformation, in which the shape of the protein changes from that best described by a prolate ellipsoid to a flexible structure best described by a Debye random coil, is physiologically relevant because a weak lysine binding site regulates the activation of plasminogen.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- A Plasminogen-Like Protease in Thyroid Rough Microsomes Degrades Thyroperoxidase and Thyroglobulin.
- A. Giraud, P.-J. Lejeune, J. Barbaria, and B. Mallet (2007)
Endocrinology
148, 2886-2893
| Abstract »
| Full Text »
| PDF »
- Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen.
- V. Hurmalainen, S. Edelman, J. Antikainen, M. Baumann, K. Lahteenmaki, and T. K. Korhonen (2007)
Microbiology
153, 1112-1122
| Abstract »
| Full Text »
| PDF »
- Resolution of Conformational Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase.
- P. D. Boxrud, I. M. Verhamme, and P. E. Bock (2004)
J. Biol. Chem.
279, 36633-36641
| Abstract »
| Full Text »
| PDF »
- Coupling of Conformational and Proteolytic Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase.
- P. D. Boxrud and P. E. Bock (2004)
J. Biol. Chem.
279, 36642-36649
| Abstract »
| Full Text »
| PDF »
- Characterization of plasminogen as an adhesive ligand for integrins {alpha}M{beta}2 (Mac-1) and {alpha}5{beta}1 (VLA-5).
- V. K. Lishko, V. V. Novokhatny, V. P. Yakubenko, H. V. Skomorovska-Prokvolit, and T. P. Ugarova (2004)
Blood
104, 719-726
| Abstract »
| Full Text »
| PDF »
- {alpha} Domain Deletion Converts Streptokinase into a Fibrin-dependent Plasminogen Activator through Mechanisms Akin to Staphylokinase and Tissue Plasminogen Activator.
- I. Y. Sazonova, B. R. Robinson, I. P. Gladysheva, F. J. Castellino, and G. L. Reed (2004)
J. Biol. Chem.
279, 24994-25001
| Abstract »
| Full Text »
| PDF »
- A Plasminogen-like Protein Selectively Degrades Stearoyl-CoA Desaturase in Liver Microsomes.
- F. S. Heinemann, G. Korza, and J. Ozols (2003)
J. Biol. Chem.
278, 42966-42975
| Abstract »
| Full Text »
| PDF »
- Functional map and domain structure of MET, the product of the c-met protooncogene and receptor for hepatocyte growth factor/scatter factor.
- E. Gherardi, M. E. Youles, R. N. Miguel, T. L. Blundell, L. Iamele, J. Gough, A. Bandyopadhyay, G. Hartmann, and P. J. G. Butler (2003)
PNAS
100, 12039-12044
| Abstract »
| Full Text »
| PDF »
- Domain Truncation Studies Reveal That the Streptokinase-Plasmin Activator Complex Utilizes Long Range Protein-Protein Interactions with Macromolecular Substrate to Maximize Catalytic Turnover.
- V. Sundram, J. S. Nanda, K. Rajagopal, J. Dhar, A. Chaudhary, and G. Sahni (2003)
J. Biol. Chem.
278, 30569-30577
| Abstract »
| Full Text »
| PDF »
- A Ligand-induced Conformational Change in Apolipoprotein(a) Enhances Covalent Lp(a) Formation.
- L. Becker, B. A. Webb, S. Chitayat, M. E. Nesheim, and M. L. Koschinsky (2003)
J. Biol. Chem.
278, 14074-14081
| Abstract »
| Full Text »
| PDF »
- Regulation of Tissue Plasminogen Activator Activity by Cells. DOMAINS RESPONSIBLE FOR BINDING AND MECHANISM OF STIMULATION.
- V. Sinniger, R. E. Merton, P. Fabregas, J. Felez, and C. Longstaff (1999)
J. Biol. Chem.
274, 12414-12422
| Abstract »
| Full Text »
| PDF »
- Expression of Plasminogen Activator Pla of Yersinia pestis Enhances Bacterial Attachment to the Mammalian Extracellular Matrix.
- K. Lahteenmaki, R. Virkola, A. Saren, L. Emody, and T. K. Korhonen (1998)
Infect. Immun.
66, 5755-5762
| Abstract »
| Full Text »
| PDF »
- Identification of Two Laminin-Binding Fimbriae, the Type 1 Fimbria of Salmonella enterica Serovar Typhimurium and the G Fimbria of Escherichia coli, as Plasminogen Receptors.
- M. Kukkonen, S. Saarela, K. Lahteenmaki, U. Hynonen, B. Westerlund-Wikstrom, M. Rhen, and T. K. Korhonen (1998)
Infect. Immun.
66, 4965-4970
| Abstract »
| Full Text »
| PDF »
- Kringle 2 Mediates High Affinity Binding of Plasminogen to an Internal Sequence in Streptococcal Surface Protein PAM.
- A. C. Wistedt, H. Kotarsky, D. Marti, U. Ringdahl, F. J. Castellino, J. Schaller, and U. Sjobring (1998)
J. Biol. Chem.
273, 24420-24424
| Abstract »
| Full Text »
| PDF »
- Tissue Factor Regulates Plasminogen Binding and Activation.
- Z. Fan, P. J. Larson, J. Bognacki, P.N. Raghunath, J. E. Tomaszewski, A. Kuo, G. Canziani, I. Chaiken, D. B. Cines, and A. A.-R. Higazi (1998)
Blood
91, 1987-1998
| Abstract »
| Full Text »
| PDF »
- Production and Characterization of Recombinant Human Plasminogen(S741C-Fluorescein). A NOVEL APPROACH TO STUDY ZYMOGEN ACTIVATION WITHOUT GENERATION OF ACTIVE PROTEASE.
- A. J.G. Horrevoets, H. Pannekoek, and M. E. Nesheim (1997)
J. Biol. Chem.
272, 2176-2182
| Abstract »
| Full Text »
| PDF »
- Complement C5b-9 Increases Plasminogen Binding and Activation on Human Endothelial Cells.
- V. J. Christiansen, P. J. Sims, and K. K. Hamilton (1997)
Arterioscler. Thromb. Vasc. Biol.
17, 164-171
| Abstract »
| Full Text »
- Interactions between Staphylokinase, Plasmin(ogen), and Fibrin. STAPHYLOKINASE DISCRIMINATES BETWEEN FREE PLASMINOGEN AND PLASMINOGEN BOUND TO PARTIALLY DEGRADED FIBRIN.
- D. V. Sakharov, H. R. Lijnen, and D. C. Rijken (1996)
J. Biol. Chem.
271, 27912-27918
| Abstract »
| Full Text »
| PDF »
- A Steady-state Template Model That Describes the Kinetics of Fibrin-stimulated [Glu1]- and [Lys78]Plasminogen Activation by Native tissue-type Plasminogen Activator and Variants That Lack Either the Finger or Kringle-2 Domain.
- A. J.G. Horrevoets, H. Pannekoek, and M. E. Nesheim (1996)
J. Biol. Chem.
272, 2183-2191
| Abstract »
| Full Text »
| PDF »
- Analogs of Human Plasminogen That Are Labeled with Fluorescence Probes at the Catalytic Site of the Zymogen.
- P. E. Bock, D. E. Day, I. M. A. Verhamme, M. M. Bernardo, S. T. Olson, and J. D. Shore (1996)
J. Biol. Chem.
271, 1072-1080
| Abstract »
| Full Text »
| PDF »
- Structural Features Mediating Fibrin Selectivity of Vampire Bat Plasminogen Activators.
- P. Bringmann, D. Gruber, A. Liese, L. Toschi, Jör. Krätzschmar, W.-D. Schleuning, and P. Donner (1995)
J. Biol. Chem.
270, 25596-25603
| Abstract »
| Full Text »
| PDF »
- Location of the Major [IMAGE]-([IMAGE]-Glutamyl)lysyl Cross-linking Site in Transglutaminase-modified Human Plasminogen.
- E. Bendixen, P. C. Harpel, and L. Sottrup-Jensen (1995)
J. Biol. Chem.
270, 17929-17933
| Abstract »
| Full Text »
| PDF »
- The Activation-resistant Conformation of Recombinant Human Plasminogen Is Stabilized by Basic Residues in the Amino-terminal Hinge Region.
- A. J. G. Horrevoets, A. E. Smilde, J. C. Fredenburgh, H. Pannekoek, and M. E. Nesheim (1995)
J. Biol. Chem.
270, 15770-15776
| Abstract »
| Full Text »
| PDF »
- Neutron scattering: progress and prospects.
- J. Axe (1991)
Science
252, 795-802
| Abstract »
| PDF »
- Spatial Regulation and Activity Modulation of Plasmin by High Affinity Binding to the G domain of the alpha 3 Subunit of Laminin-5.
- L. E. Goldfinger, L. Jiang, S. B. Hopkinson, M. S. Stack, and J. C. R. Jones (2000)
J. Biol. Chem.
275, 34887-34893
| Abstract »
| Full Text »
| PDF »
|
|
