Structure of leech derived tryptase inhibitor (LDTI‐C) in solution

FEBS Letters

Habermann, Bianca¹  Auerswald, Ennes A.²  Morenweiser, Robert²  Sommerhoff, Christian P.²  Czisch, Michael¹  Engh, Richard A.¹  Holak, Tad A.¹  Mühlhahn, Peter¹ 

[1] Max-Planck-Institut für Biochemie, D-82152 Martinsried bei München, Germany;Abteilung für Klinische Chemie und Klinische Biochemie in der Chirurgischen Klinik und Poliklinik, Klinikum Innenstadt, LMU München, Germany

关键词: Tertiary structure;    Leech derived tryptase inhibitor;    Nuclear magnetic resonance;    Tryptase;    Kazal-type serine proteinase inhibitor;    LDTI;    leech derived tryptase inhibitor;    LDTI-C;    form C of the leech derived tryptase inhibitor;    P1;    P2;    P3 and P1′;    P2′;    P3′;    designate inhibitor residues amino-terminal and carboxy-terminal of the scissile peptide bond;    respectively. NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    NOESY;    two-dimensional NOE spectroscopy;    TOCSY (HOHAHA);    total correlation spectroscopy (homonuclear Hartmann-Hahn spectroscopy);    DQF-COSY;    double quantum filtered homonuclear correlated spectroscopy;    2D;    two-dimensional;    3D;    three-dimensional;    D2O;    deuterated water;    SA;    simulated annealing;    r.m.s.;    root-mean-square;   

DOI  :  10.1016/0014-5793(94)01225-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 φ angles, supplemented by 3 ϕ and 15_χ1 angles. The core of LDTI-C is very well defined and consists of a short 3₁₀-helix-loop and a short two-stranded antiparallel β-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 β-sheet via the third disulfide bridge. The binding loop in LDTI exhibits lowest energy conformations belonging to the canonical conformation of serine proteinase inhibitors.

【 授权许可】

Unknown