1HIA

KALLIKREIN COMPLEXED WITH HIRUSTASIN

Summary for 1HIA

• Entry DOI: 10.2210/pdb1hia/pdb
• Descriptor: KALLIKREIN, HIRUSTASIN, ... (4 entities in total)
• Functional Keywords: complex (protease-inhibitor), tissue kallikrein, serine protease, trypsin, psa, kinin, serpin, complex (protease-inhibitor) complex, complex (protease/inhibitor)
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted: P80302
• Total number of polymer chains: 6
• Total formula weight: 61661.45

Authors

Mittl, P.,Di Marco, S.,Gruetter, M. (deposition date: 1996-12-12, release date: 1997-12-24, Last modification date: 2024-10-23)

Primary citation

Mittl, P.R.,Di Marco, S.,Fendrich, G.,Pohlig, G.,Heim, J.,Sommerhoff, C.,Fritz, H.,Priestle, J.P.,Grutter, M.G.
A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex.
Structure, 5:253-264, 1997

PubMed Abstract: Hirustasin belongs to a class of serine protease inhibitors characterized by a well conserved pattern of cysteine residues. Unlike the closely related inhibitors, antistasin/ghilanten and guamerin, which are selective for coagulation factor Xa or neutrophil elastase, hirustasin binds specifically to tissue kallikrein. The conservation of the pattern of cysteine residues and the significant sequence homology suggest that these related inhibitors possess a similar three-dimensional structure to hirustasin.

PubMed: 9032072
DOI: 10.1016/S0969-2126(97)00183-4

Experimental method

X-RAY DIFFRACTION (2.4 Å)