2bvb
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(New page: 200px<br /><applet load="2bvb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bvb" /> '''THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEI...)
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Revision as of 06:48, 21 November 2007
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THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII
Overview
Immediately prior to invasion Toxoplasma gondii tachyzoites release a, large number of micronemal proteins (TgMICs) that participate in host cell, attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to, be identified in T. gondii and has been recently shown to be critical in, invasion. This study establishes that the N-terminal thrombospondin type I, repeat-like domains (TSR1-like) from TgMIC1 function as an independent, adhesin as well as promoting association with TgMIC4. Using the newly, solved three-dimensional structure of the C-terminal domain of TgMIC1 we, have identified a novel Galectin-like fold that does not possess, carbohydrate binding properties and redefines the architecture of TgMIC1., Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism, for successful exit from the early secretory compartments and for, subsequent trafficking of the complex to the micronemes.
About this Structure
2BVB is a Single protein structure of sequence from Toxoplasma gondii. Full crystallographic information is available from OCA.
Reference
A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex., Saouros S, Edwards-Jones B, Reiss M, Sawmynaden K, Cota E, Simpson P, Dowse TJ, Jakle U, Ramboarina S, Shivarattan T, Matthews S, Soldati-Favre D, J Biol Chem. 2005 Nov 18;280(46):38583-91. Epub 2005 Sep 15. PMID:16166092
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