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Protein Science (2004), 13:1735-1749. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Determinants of quaternary association in legume lectins

K.V. Brinda, Nivedita Mitra, Avadhesha Surolia and Saraswathi Vishveshwara

Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India

(RECEIVED January 23, 2004; FINAL REVISION April 18, 2004; ACCEPTED April 19, 2004)



Abstract

It is well known that the sequence of amino acids in proteins code for its tertiary structure. It is also known that there exists a relationship between sequence and the quaternary structure of proteins. The question addressed here is whether the nature of quaternary association can be predicted from the sequence, similar to the three-dimensional structure prediction from the sequence. The class of proteins called legume lectins is an interesting model system to investigate this problem, because they have very high sequence and tertiary structure homology, with diverse forms of quaternary association. Hence, we have used legume lectins as a probe in this paper to (1) gain novel insights about the relationship between sequence and quaternary structure; (2) identify the sequence motifs that are characteristic of a given type of quaternary association; and (3) predict the quaternary association from the sequence motif.

Keywords: computational protein structure analysis; quaternary association; oligomerization; legume lectins; graph-spectral method; interface amino acid clusters; conserved amino acid clusters

Reprint requests to: Saraswathi Vishveshwara, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India; e-mail: sv{at}mbu.iisc.ernet.in; fax: 91-80-23600535.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04651004.


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