1DDJ

CRYSTAL STRUCTURE OF HUMAN PLASMINOGEN CATALYTIC DOMAIN

Summary for 1DDJ

• Entry DOI: 10.2210/pdb1ddj/pdb
• Descriptor: PLASMINOGEN (2 entities in total)
• Functional Keywords: plasminogen, catalytic domain, blood clotting
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00747
• Total number of polymer chains: 4
• Total formula weight: 108320.54

Authors

Wang, X.,Terzyan, S.,Tang, J.,Loy, J.,Lin, X.,Zhang, X. (deposition date: 1999-11-10, release date: 2000-02-18, Last modification date: 2024-10-30)

Primary citation

Wang, X.,Terzyan, S.,Tang, J.,Loy, J.A.,Lin, X.,Zhang, X.C.
Human plasminogen catalytic domain undergoes an unusual conformational change upon activation.
J.Mol.Biol., 295:903-914, 2000

PubMed Abstract: Activation of the serine protease plasmin from its zymogen, plasminogen, is the key step in fibrinolysis leading to blood clot dissolution. It also plays critical roles in cell migration, such as in tumor metastasis. Here, we report the crystal structure of an inactive S741A mutant of human plasminogen catalytic domain at 2.0 A resolution. This structure permits a direct comparison with that of the plasmin catalytic unit. Unique conformational differences are present between these two structures that are not seen in other zymogen-enzyme pairs of the trypsin family. The functional significance of these differences and the structural basis of plasminogen activation is discussed in the light of this new structure.

PubMed: 10656799
DOI: 10.1006/jmbi.1999.3397

Experimental method

X-RAY DIFFRACTION (2 Å)