1ATH

THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS

Summary for 1ATH

• Entry DOI: 10.2210/pdb1ath/pdb
• Descriptor: ANTITHROMBIN III (1 entity in total)
• Functional Keywords: human antithrombin-iii
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space: P01008
• Total number of polymer chains: 2
• Total formula weight: 98202.03

Authors

Schreuder, H.A.,Hol, W.G.J. (deposition date: 1993-12-14, release date: 1995-02-07, Last modification date: 2024-10-30)

Primary citation

Schreuder, H.A.,de Boer, B.,Dijkema, R.,Mulders, J.,Theunissen, H.J.,Grootenhuis, P.D.,Hol, W.G.
The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions.
Nat.Struct.Biol., 1:48-54, 1994

PubMed Abstract: Antithrombin is a member of the serine proteinase inhibitor (serpin) family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive site loop is completely exposed and in an alpha-helical conformation. However, in neither conformation can the reactive site loop bind to target proteinases. Here we report the structure of an intact and cleaved human antithrombin complex. The intact reactive site loop is in a novel conformation that seems well suited for interaction with proteinases such as thrombin and blood coagulation factor Xa.

PubMed: 7656006
DOI: 10.1038/nsb0194-48

Experimental method

X-RAY DIFFRACTION (3.2 Å)