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4d94
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==Crystal Structure of TEP1r== |
| + | <StructureSection load='4d94' size='340' side='right' caption='[[4d94]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4d94]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D94 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d93|4d93]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tep1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae])</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=4d94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d94 RCSB], [http://www.ebi.ac.uk/pdbsum/4d94 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thioester-containing protein 1 (TEP1) is a central component in the innate immune response of Anopheles gambiae to Plasmodium infection. Two classes of TEP1 alleles, TEP1*S and TEP1*R, are found in both laboratory strains and wild isolates, related by a greater or lesser susceptibility, respectively to both P. berghei and P. falciparum infection. We report the crystal structure of the full-length TEP1*S1 allele which, while similar to the previously determined structure of full-length TEP1*R1, displays flexibility in the N-terminal fragment comprising domains MG1-MG6. Amino acid differences between TEP1*R1 and TEP1*S1 are localized to the TED-MG8 domain interface that protects the thioester bond from hydrolysis and structural changes are apparent at this interface. As a consequence cleaved TEP1*S1 (TEP1*S1(cut)) is significantly more susceptible to hydrolysis of its intramolecular thioester bond than TEP1*R1(cut). TEP1*S1(cut) is stabilized in solution by the heterodimeric LRIM1/APL1C complex, which preserves the thioester bond within TEP1*S1(cut). These results suggest a mechanism by which selective pressure on the TEP1 gene results in functional variation that may influence the vector competence of A. gambiae towards Plasmodium infection. | ||
| - | + | Molecular Basis for Genetic Resistance of Anopheles gambiae to Plasmodium: Structural Analysis of TEP1 Susceptible and Resistant Alleles.,Le BV, Williams M, Logarajah S, Baxter RH PLoS Pathog. 2012 Oct;8(10):e1002958. doi: 10.1371/journal.ppat.1002958. Epub, 2012 Oct 4. PMID:23055931<ref>PMID:23055931</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Anopheles gambiae]] | [[Category: Anopheles gambiae]] | ||
| - | [[Category: Baxter, R H.G | + | [[Category: Baxter, R H.G]] |
| - | [[Category: Le, B V | + | [[Category: Le, B V]] |
| - | [[Category: Logarajah, S | + | [[Category: Logarajah, S]] |
| - | [[Category: Williams, M | + | [[Category: Williams, M]] |
[[Category: Component of innate immune response by the opsinization and melanization of pathogen]] | [[Category: Component of innate immune response by the opsinization and melanization of pathogen]] | ||
[[Category: Full-length protein]] | [[Category: Full-length protein]] | ||
Revision as of 08:21, 20 January 2015
Crystal Structure of TEP1r
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