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The three-dimensional solution structure of human stefin A

J R Martin¹, C J Craven, R Jerala

¹Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.

Journal of Molecular Biology

|February 17, 1995

Summary

The three-dimensional structure of human stefin A reveals a stable fold with mobile regions crucial for proteinase binding. These flexible areas in stefin A differ from its bound homolog, stefin B, highlighting distinct interaction mechanisms.

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Area of Science:

Structural biology
Biochemistry
Molecular dynamics

Background:

Stefin A is a cysteine proteinase inhibitor.
Understanding its structure is key to protein-protein interactions.

Purpose of the Study:

Determine the 3D solution structure of recombinant human stefin A.
Compare its structure to homologous proteins in complex with proteinases.

Main Methods:

Simulated annealing protocol.
1H and 15N Heteronuclear Magnetic Resonance (HMR) spectroscopy.
Analysis of 1113 distance and angle constraints.

Main Results:

A family of 17 conformers representing the solution structure.
A defined fold of five anti-parallel beta-strands around a central alpha-helix.

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Identified two mobile regions (N-terminal residues and second binding loop) with conformational heterogeneity.

Conclusions:

Human stefin A possesses a stable global fold but exhibits flexibility in key binding regions.
These flexible regions differ from the bound conformation of homologous stefin B, suggesting distinct proteinase binding mechanisms.