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Published online before print December 2, 2004, 10.1110/ps.04945605
Protein Science (2005), 14:169-175. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Structure of rhodocetin reveals noncovalently bound heterodimer interface

Palasingam Paaventhan1, Chunguang Kong2, Jeremiah S. Joseph3, Max C.M. Chung4 and Prasanna R. Kolatkar1

1 Genome Institute of Singapore, Singapore 138672
2 Institute of Molecular and Cell Biology, Singapore 117609
3 The Scripps Research Institute, La Jolla, California 92037, USA
4 Department of Biochemistry Faculty of Medicine, National University of Singapore, Singapore 117597

(RECEIVED June 22, 2004; FINAL REVISION August 30, 2004; ACCEPTED August 30, 2004)

Rhodocetin is a unique heterodimer consisting of {alpha}- and {beta}-subunits of 133 and 129 residues, respectively. The molecule, purified from the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge, unlike all the other Ca2+-dependent lectin-like proteins. We report here the 1.9 Å resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.

Keywords: platelet aggregation inhibitor; Calloselasma rhodostoma; heterodimer; C-type lectin-like protein; domain swapping

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04945605.

Reprint requests to: Prasanna R. Kolatkar, Genome Institute of Singapore, Singapore 138672; e-mail: kolatkarp{at}gis.a-star.edu.sg; fax: +(65) 6478-9058.


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