4okr
From Proteopedia
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| - | + | ==Structures of Toxoplasma gondii MIC2== | |
| - | === | + | <StructureSection load='4okr' size='340' side='right' caption='[[4okr]], [[Resolution|resolution]] 2.60Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4okr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oku|4oku]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGVEG_201780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4okr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4okr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4okr RCSB], [http://www.ebi.ac.uk/pdbsum/4okr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Micronemal protein 2 (MIC2) is the key adhesin that supports gliding motility and host cell invasion by Toxoplasma gondii. With a von Willebrand factor A (VWA) domain and six thrombospondin repeat domains (TSR1-6) in its ectodomain, MIC2 connects to the parasite actomyosin system through its cytoplasmic tail. MIC2-associated protein (M2AP) binds noncovalently to the MIC2 ectodomain. MIC2 and M2AP are stored in micronemes as proforms. We find that the MIC2-M2AP ectodomain complex is a highly elongated 1:1 monomer with M2AP bound to the TSR6 domain. Crystal structures of N-terminal fragments containing the VWA and TSR1 domains for proMIC2 and MIC2 reveal a closed conformation of the VWA domain and how it associates with the TSR1 domain. A long, proline-rich, disulfide-bonded pigtail loop in TSR1 overlaps the VWA domain. Mannose alpha-C-linked to Trp-276 in TSR1 has an unusual (1)C4 chair conformation. The MIC2 VWA domain includes a mobile alpha5-helix and a 22-residue disordered region containing two disulfide bonds in place of an alpha6-helix. A hydrophobic residue in the prodomain binds to a pocket adjacent to the alpha7-helix that pistons in opening of the VWA domain to a putative high-affinity state. | ||
| - | + | Structures of the Toxoplasma gliding motility adhesin.,Song G, Springer TA Proc Natl Acad Sci U S A. 2014 Apr 1;111(13):4862-7. doi:, 10.1073/pnas.1403059111. Epub 2014 Mar 17. PMID:24639528<ref>PMID:24639528</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Toxgo]] | [[Category: Toxgo]] | ||
| - | [[Category: Song, G | + | [[Category: Song, G]] |
| - | [[Category: Springer, T A | + | [[Category: Springer, T A]] |
[[Category: Adhesin]] | [[Category: Adhesin]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 07:11, 15 February 2015
Structures of Toxoplasma gondii MIC2
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