1SEK

THE STRUCTURE OF ACTIVE SERPIN K FROM MANDUCA SEXTA AND A MODEL FOR SERPIN-PROTEASE COMPLEX FORMATION

Summary for 1SEK

• Entry DOI: 10.2210/pdb1sek/pdb
• Descriptor: SERPIN K (2 entities in total)
• Functional Keywords: serine protease inhibitor, serpin, protease
• Biological source: Manduca sexta (tobacco hornworm)
• Cellular location: Secreted, extracellular space: P14754
• Total number of polymer chains: 1
• Total formula weight: 42273.17

Authors

Li, J.,Wang, Z.,Canagarajah, B.,Jiang, H.,Kanost, M.,Goldsmith, E.J. (deposition date: 1998-03-06, release date: 1999-03-23, Last modification date: 2024-02-14)

Primary citation

Li, J.,Wang, Z.,Canagarajah, B.,Jiang, H.,Kanost, M.,Goldsmith, E.J.
The structure of active serpin 1K from Manduca sexta.
Structure Fold.Des., 7:103-109, 1999

PubMed Abstract: The reactive center loops (RCL) of serpins undergo large conformational changes triggered by the interaction with their target protease. Available crystallographic data suggest that the serpin RCL is polymorphic, but the relevance of the observed conformations to the competent active structure and the conformational changes that occur on binding target protease has remained obscure. New high-resolution data on an active serpin, serpin 1K from the moth hornworm Manduca sexta, provide insights into how active serpins are stabilized and how conformational changes are induced by protease binding.

PubMed: 10368276
DOI: 10.1016/S0969-2126(99)80013-6

Experimental method

X-RAY DIFFRACTION (2.1 Å)