2bvb
From Proteopedia
(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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| - | [[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size=" | + | [[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bvb" /> | caption="2bvb" /> | ||
'''THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII'''<br /> | '''THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Immediately prior to invasion Toxoplasma gondii tachyzoites release a | + | 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== | ==About this Structure== | ||
| - | 2BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http:// | + | 2BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: microneme]] | [[Category: microneme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:01 2008'' |
Revision as of 14:42, 21 February 2008
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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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