Structure-function-folding relationships and native energy landscape of dynein light chain protein: nuclear magnetic resonance insights.

P M Krishna Mohan, Ramakrishna V Hosur

Journal: Journal of biosciences 2009;34(3):465-79

PMID: 19805907

Abstract

The detailed characterization of the structure, dynamics and folding process of a protein is crucial for understanding the biological functions it performs. Modern biophysical and nuclear magnetic resonance (NMR) techniques have provided a way to obtain accurate structural and thermodynamic information on various species populated on the energy landscape of a given protein. In this context, we review here the structure-function-folding relationship of an important protein, namely, dynein light chain protein (DLC8). DLC8, the smallest subunit of the dynein motor complex, acts as a cargo adaptor. The protein exists as a dimer under physiological conditions and dissociates into a pure monomer below pH 4. Cargo binding occurs at the dimer interface. Dimer stability and relay of perturbations through the dimer interface are anticipated to be playing crucial roles in the variety of functions the protein performs. NMR investigations have provided great insights into these aspects of DLC8 in recent years.

Address: Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India.

DOI: 10.1007/s12038-009-0052-0

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MeSH Terms: Amino Acid Sequence, Cytoplasmic Dyneins, Dimerization, Hot Temperature, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oligopeptides, Physical Phenomena, Protein Binding, Protein Conformation, Protein Denaturation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship, Thermodynamics