2bbx
From Proteopedia
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NMR solution structure of the TSR domain of malaria TRAP protein
Overview
Thrombospondin-related anonymous protein, TRAP, has a critical role in the, hepatocyte invasion step of Plasmodium sporozoites, the transmissible form, of the parasite causing malaria. The extracellular domains of this, sporozoite surface protein interact with hepatocyte surface receptors, whereas its intracellular domain acts as a link to the sporozoite, actomyosin motor system. Liver heparan sulfate proteoglycans have been, identified as potential ligands for TRAP. Proteoglycan binding has been, associated with the A- and TSR domains of TRAP. We present the solution, NMR structure of the TSR domain of TRAP and a chemical shift mapping study, of its heparin binding epitope. The domain has an elongated structure, stabilized by an array of tryptophan and arginine residues as well as, disulfide bonds. The fold is very similar to those of thrombospondin, type-1 (TSP-1) and F-spondin TSRs. The heparin binding site of TRAP-TSR is, located in the N-terminal half of the structure, the layered side chains, forming an integral part of the site. The smallest heparin fragment, capable of binding to TRAP-TSR is a tetrasaccharide.
About this Structure
2BBX is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site., Tossavainen H, Pihlajamaa T, Huttunen TK, Raulo E, Rauvala H, Permi P, Kilpelainen I, Protein Sci. 2006 Jul;15(7):1760-8. PMID:16815922
Page seeded by OCA on Wed Nov 21 08:42:41 2007
