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3oja
From Proteopedia
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| - | {{STRUCTURE_3oja| PDB=3oja | SCENE= }} | ||
| - | ===Crystal structure of LRIM1/APL1C complex=== | ||
| - | {{ABSTRACT_PUBMED_20826443}} | ||
| - | == | + | ==Crystal structure of LRIM1/APL1C complex== |
| - | [[3oja]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <StructureSection load='3oja' size='340' side='right' caption='[[3oja]], [[Resolution|resolution]] 2.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3oja]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anoga Anoga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OJA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGAP006348, LRIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 ANOGA]), AGAP007033, APL1C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 ANOGA])</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=3oja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oja OCA], [http://pdbe.org/3oja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oja RCSB], [http://www.ebi.ac.uk/pdbsum/3oja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oja ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/3oja_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3oja ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The leucine-rich repeat (LRR) proteins LRIM1 and APL1C control the function of the complement-like protein TEP1 in Anopheles mosquitoes. The molecular structure of LRIM1 and APL1C and the basis of their interaction with TEP1 represent a new type of innate immune complex. The LRIM1/APL1C complex specifically binds and solubilizes a cleaved form of TEP1 without an intact thioester bond. The LRIM1 and APL1C LRR domains have a large radius of curvature, glycosylated concave face, and a novel C-terminal capping motif. The LRIM1/APL1C complex is a heterodimer with a single intermolecular disulfide bond. The structure of the LRIM1/APL1C heterodimer reveals an interface between the two LRR domains and an extensive C-terminal coiled-coil domain. We propose that a cleaved form of TEP1 may act as a convertase for activation of other TEP1 molecules and that the LRIM1/APL1C heterodimer regulates formation of this TEP1 convertase. | ||
| - | + | A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae.,Baxter RH, Steinert S, Chelliah Y, Volohonsky G, Levashina EA, Deisenhofer J Proc Natl Acad Sci U S A. 2010 Sep 8. PMID:20826443<ref>PMID:20826443</ref> | |
| - | <ref | + | |
| - | [[Category: | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Baxter, R H.G | + | </div> |
| - | [[Category: Deisenhofer, J | + | <div class="pdbe-citations 3oja" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Anoga]] | ||
| + | [[Category: Baxter, R H.G]] | ||
| + | [[Category: Deisenhofer, J]] | ||
[[Category: Coiled-coil]] | [[Category: Coiled-coil]] | ||
[[Category: Helix-loop-helix]] | [[Category: Helix-loop-helix]] | ||
[[Category: Leucine-rich repeat]] | [[Category: Leucine-rich repeat]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
Current revision
Crystal structure of LRIM1/APL1C complex
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