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Licensed Unlicensed Requires Authentication Published by De Gruyter August 1, 2007

The structure of CMS2MS2, a mitogenic protein isolated from Carica candamarcensis

  • Marco Túlio R. Gomes , Marcelo P. Bemquerer , Miriam Tereza P. Lopes , Michael Richardson , Sergio Oyama Júnior and Carlos E. Salas
From the journal Biological Chemistry
https://doi.org/10.1515/BC.2007.083

Abstract

In a recent study we showed that two proteinases (CMS2MS2 and CMS2MS3) from Carica candamarcensis enhance mammalian cell proliferation. The aim of the present study is the determination of the primary structure of CMS2MS2 and prediction of its three-dimensional structure. The protein contains 214 residues, including the catalytic triad composed of Cys25, His159, and Asn175. A phylogenetic tree analysis demonstrated that CMS2MS2 ranks closer to chymopapain than to papain. The overall predicted three-dimensional structure is similar to proteinases from the papain family. These results suggest that minor structural differences within CMS2MS2 must account for its proliferative action.

Keywords: Caricaceae; cysteine proteinase; latex; mitogenic
Corresponding author
Received: 2007-2-2
Accepted: 2007-4-17
Published Online: 2007-08-01

©2007 by Walter de Gruyter Berlin New York

From the journal
Biological Chemistry
Biological Chemistry
Volume 388 Issue 8
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