View source for 2mpo


==Structural basis of Toxoplasma gondii MIC2-Associated Protein interaction with MIC2==
<StructureSection load='2mpo' size='340' side='right'caption='[[2mpo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mpo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpo OCA], [https://pdbe.org/2mpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mpo RCSB], [https://www.ebi.ac.uk/pdbsum/2mpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q967S9_TOXGO Q967S9_TOXGO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Toxoplasma gondii parasites must actively invade host cells to propagate. Secretory microneme proteins have been shown to be important for both gliding motility and active invasion. MIC2-M2AP is a protein complex that is essential for productive motility and rapid invasion by binding to host cell surface receptors. To investigate the architecture of the MIC2 and M2AP complex, we identified the minimal domains sufficient for interaction and solved the NMR solution structure of the globular domain of M2AP. We found that M2AP adopts a modified galectin fold similar to the C-terminal domain of another microneme protein, MIC1. NMR and immunoprecipitation analyses implicated hydrophobic residues on one face of the M2AP galectin fold in binding to the membrane proximal sixth thrombospondin type I repeat domain of MIC2. Our findings provide a second example of a galectin fold adapted for microneme protein-protein interactions and suggest a conserved strategy for the assembly and folding of diverse protein complexes.

Structural basis of Toxoplasma gondii MIC2-associated protein interaction with MIC2.,Huynh MH, Liu B, Henry M, Liew L, Matthews SJ, Carruthers VB J Biol Chem. 2015 Jan 16;290(3):1432-41. doi: 10.1074/jbc.M114.613646. Epub 2014 , Nov 19. PMID:25411252<ref>PMID:25411252</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mpo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Toxoplasma gondii]]
[[Category: Liu B]]
[[Category: Matthews S]]