Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex.

The 2.4 A crystal structure (R = 0.180) of the serine protease inhibitor ecotin was determined in a complex with trypsin. Ecotin's dimer structure provides a second discrete and distal binding site for trypsin and, as shown by modelling experiments, other serine proteases. The second site is approxi...

Celý popis

Podrobná bibliografie

Vydáno v:	EMBO J
Hlavní autoři:	McGrath, M E, Erpel, T, Bystroff, C, Fletterick, R J
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Nature Publishing Group 1994
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC394978/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8156987/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1994.tb06411.x
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!