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1ath
From Proteopedia
| 1ath, resolution 3.20Å () | |||||||||
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| Domains: | antithrombin-III_like | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS
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.
The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions., Schreuder HA, de Boer B, Dijkema R, Mulders J, Theunissen HJ, Grootenhuis PD, Hol WG, Nat Struct Biol. 1994 Jan;1(1):48-54. PMID:7656006
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ATH is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Schreuder HA, de Boer B, Dijkema R, Mulders J, Theunissen HJ, Grootenhuis PD, Hol WG. The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat Struct Biol. 1994 Jan;1(1):48-54. PMID:7656006
Page seeded by OCA on Tue Feb 17 17:48:14 2009
