Structure of leech derived tryptase inhibitor (LDTI-C) in solution.
The three-dimensional solution structure of the leech derived tryptase inhibitor form C (LDTI-C), an inhibitor of 46 amino acids which contains 3 disulfide bridges, has been determined using 2D NMR spectroscopy. The 3D structure was determined on the basis of 262 interresidue interproton distance constraints derived from nuclear Overhauser enhancement measurements and 25 phi angles, supplemented by 3 psi and 15 chi 1 angles. The core of LDTI-C is very well defined and consists of a short 3(10)-helix-loop and a short two-stranded antiparallel beta-sheet between residues 13-14 and 20-21. The N-terminus is fixed to the core by two disulfide bridges, while the C-terminus is connected to the beta-sheet via the third disulfide bridge. The binding loop in LDTI exhibits lowest energy conformations belonging to the canonical conformation of serine proteinase inhibitors.
Mühlhahn
P
P
Max-Planck-Institut für Biochemie, Martinsried bei München, Germany.
Czisch
M
M
Morenweiser
R
R
Habermann
B
B
Engh
R A
RA
Sommerhoff
C P
CP
Auerswald
E A
EA
Holak
T A
TA
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003198:Computer Simulation; D005813:Genes, Synthetic; D007865:Leeches / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D012996:Solutions; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000737:chemistry
D011480:Protease Inhibitors; D011506:Proteins; D011994:Recombinant Proteins; D012996:Solutions; C090901:leech-derived tryptase inhibitor C; D014359:Trypsin Inhibitor, Kazal Pancreatic