Journal
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 165, Issue 2, Pages 153-161Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2009.01.015
Keywords
alpha-Helical coiled coil; Oligomerization; Protein structure; Plasmodium falciparum
Categories
Funding
- National Institutes of Health, NIBIB
Ask authors/readers for more resources
Proteins located on the surface of the pathogenic malaria parasite Plasmodium falciparum are objects of intensive studies due to their important role in the invasion of human cells and the accessibility to host antibodies thus making these proteins attractive vaccine candidates. One of these proteins, merozoite surface protein 3 (MSP3) represents a leading component among vaccine candidates; however, little is known about its structure and function. Our biophysical studies suggest that the 40 residue C-terminal domain of MSP3 protein self-assembles into a four-stranded alpha-helical coiled coil structure where alpha-helices are packed side-by-side. A bioinformatics analysis provides an extended list of known and putative proteins from different species of Plasmodium which have such MSP3-like C-terminal domains. This finding allowed us to extend some conclusions of our studies to a larger group of the malaria surface proteins. Possible structural and functional roles of these highly conserved oligomerization domains in the intact merozoite surface proteins are discussed. (C) 2009 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available