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Building protein structure and function from modular units
1Department of Biochemistry, University of Oxford, UK.
Trends in Biotechnology
|May 1, 1994
Summary
This review explores recent structural studies on protein modules, focusing on X-ray crystallography and NMR. Understanding these protein domains aids in comprehending the function of complex cellular proteins.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Multicellular proteins are often modular, composed of distinct autonomously folding domains.
- Knowledge of individual module structures and some module pairs is increasing.
- Many functionally important proteins are large, membrane-bound, and glycosylated.
Purpose of the Study:
- To review recent advancements in the structural determination of protein modules.
- To highlight the application of X-ray crystallography and Nuclear Magnetic Resonance (NMR) techniques.
- To discuss the implications of module structures for understanding intact protein function.
Main Methods:
- X-ray crystallography
- Nuclear Magnetic Resonance (NMR) spectroscopy
- Analysis of 'dissected' protein modules
Main Results:
- Structural data is available for numerous individual protein modules and some pairs.
- Recent studies have focused on modules from large, membrane-bound, and glycosylated proteins.
- Structural insights have been gained for modules involved in cell adhesion, clotting, fibrinolysis, and signaling.
Conclusions:
- Structural information on individual protein modules provides a basis for understanding complex protein architectures.
- The study of dissected modules aids in elucidating the function of intact, often large and complex, proteins.
- Recent structural work offers new perspectives on proteins critical for cellular processes.