2bvb

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[[Image:2bvb.png|left|200px]]
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==THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII==
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<StructureSection load='2bvb' size='340' side='right' caption='[[2bvb]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bvb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BVB FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bvb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bvb RCSB], [http://www.ebi.ac.uk/pdbsum/2bvb PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2bvb| PDB=2bvb | SCENE= }}
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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<ref>PMID:16166092</ref>
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===THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16166092}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2bvb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:016166092</ref><references group="xtra"/>
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[[Category: Toxoplasma gondii]]
[[Category: Toxoplasma gondii]]
[[Category: Cota, E.]]
[[Category: Cota, E.]]

Revision as of 07:01, 9 June 2014

THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII

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