1ATD

HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE

Summary for 1ATD

• Entry DOI: 10.2210/pdb1atd/pdb
• Descriptor: ASCARIS TRYPSIN INHIBITOR (1 entity in total)
• Functional Keywords: proteinase inhibitor(trypsin)
• Biological source: Ascaris suum (pig roundworm)
• Total number of polymer chains: 1
• Total formula weight: 6807.85

Authors

Clore, G.M.,Grasberger, B.L.,Gronenborn, A.M. (deposition date: 1994-05-20, release date: 1994-08-31, Last modification date: 2024-10-09)

Primary citation

Grasberger, B.L.,Clore, G.M.,Gronenborn, A.M.
High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site.
Structure, 2:669-678, 1994

PubMed Abstract: The Ascaris trypsin inhibitor (ATI) is a member of a new family of serine protease inhibitors isolated from the helminthic worm Ascaris lumbricoides var suum. This family comprises five chymotrypsin/elastase inhibitors and one trypsin inhibitor. Members are characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues.

PubMed: 7922043
DOI: 10.1016/S0969-2126(00)00067-8

Experimental method

SOLUTION NMR