ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins

Moses, Prabu M and Suguna, K and Vijayan, M (1999) Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins. In: Proteins, 35 (1). pp. 58-69.

[img] PDF
Variability_in_Quaternary_Association.pdf
Restricted to Registered users only

Download (287Kb) | Request a copy

Abstract

Legume lectins constitute a family of proteins in which small alterations arising from sequence variations in essentially the same tertiary structure lead to large changes in quaternary association. All of them are dimers or tetramers made up of dimers. Dimerization involves side-by-side or back-to-back association of the flat six-membered beta-sheets in the protomers. Variations within these modes of dimerization can be satisfactorily described in terms of angles defining the mutual disposition of the two subunits. In all tetrameric lectins, except peanut lectin, oligomerization involves the back-to-back association of side-by-side dimers. An attempt has been made to rationalize the observed modes of oligomerization in terms of hydrophobic surface area buried on association, interaction energy and shape complementarity, by constructing energy minimised models in each of which the subunit of one legume lectin is fitted in the quaternary structure of another. The results indicate that all the three indices favor and, thus, provide a rationale for the observed arrangements. However, the discrimination provided by buried hydrophobic surface area is marginal in a few instances. The same is true, to a lesser extent, about that provided by shape complementarity. The relative values of interaction energy turns out to be a still better discriminator than the other two indices. Variability in the quaternary association of homologous proteins is a widely observed phenomenon and the present study is relevant to the general problem of protein folding.

Item Type: Journal Article
Additional Information: copyright of this article belongs to WILEY-LISS, INC.
Keywords: legume lectins;quaternary association;buried surface area; shape complementarity;interaction energy
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 11 Oct 2007
Last Modified: 19 Sep 2010 04:40
URI: http://eprints.iisc.ernet.in/id/eprint/12217

Actions (login required)

View Item View Item