A model of interdomain mobility in a multidomain protein.

A model of interdomain mobility in a multidomain protein. Research Abstract Details

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A model of interdomain mobility in a multidomain protein. Abstract Text:

Yaroslav E Ryabov,David Fushman,

Domain mobility plays an essential role in the biological function of multidomain systems. The characteristic times of domain motions fall into the interval from nano- to milliseconds, amenable to NMR studies. Proper analysis of NMR relaxation data for these systems in solution has to account for interdomain motions, in addition to the overall tumbling and local intradomain dynamics. Here we propose a model of interdomain mobility in a multidomain protein, which considers domain reorientations as exchange/interconversion between two distinct conformational states of the molecule, combined with fully anisotropic overall tumbling. Analysis of 15N-relaxation data for Lys48-linked diubiquitin at pH 4.5 and 6.8 showed that this model adequately fits the experimental data and allows characterization of both structural and motional properties of diubiquitin, thus providing information about the relative orientation of ubiquitin domains in both interconverting states. The analysis revealed that the two domains reorient on a time scale of 9-30 ns, with the amplitudes sufficient for allowing a protein ligand access to the binding sites sequestered at the interface in the closed conformation. The analysis of a possible mechanism controlling the equilibrium between the interconverting states in diubiquitin points toward protonation of His68, which results in three different charged states of the molecule, with zero, +e, and +2e net charge. Only two of the three states are noticeably populated at pH 4.5 or 6.8, which assures applicability of the two-state model to diubiquitin at these conditions. We also compare our model with the "extended model-free" approach and discuss possible future developments of the model.

A model of interdomain mobility in a multidomain protein. Publishing Authors By Initials

YE Ryabov,D Fushman,

For similar proteins: ubiquitins research abstracts see: proteins: ubiquitins research

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A model of interdomain mobility in a multidomain protein. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of the American Chemical Society

VOLUME: 129

Page Numbers: 3315-27

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 24

MONTH: 02

YEAR: 2007

A model of interdomain mobility in a multidomain protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

A model of interdomain mobility in a multidomain protein. Keywords Mesh Terms:

KEYWORDS: Ubiquitins

MESH TERMS: chemistry

Chemical & Substance for Abstract: A model of interdomain mobility in a multidomain protein. Information

Substance Name: diubiquitin conjugate

Registry Number: 0

Grant and Affiliation Information for A model of interdomain mobility in a multidomain protein.

AFFILIATION: Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland 20742, USA.

Country: United States