2mpo | pdb_00002mpo

Structural basis of Toxoplasma gondii MIC2-Associated Protein interaction with MIC2

spinqualitylabelsall models 2mpo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mpo is a 1 chain structure with sequence from Toxoplasma gondii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q967S9_TOXGO 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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