2bpd
From Proteopedia
(Difference between revisions)
| (17 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2bpd.gif|left|200px]]<br /><applet load="2bpd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2bpd, resolution 1.50Å" /> | ||
| - | '''STRUCTURE OF MURINE DECTIN-1'''<br /> | ||
| - | == | + | ==STRUCTURE OF MURINE DECTIN-1== |
| - | + | <StructureSection load='2bpd' size='340' side='right'caption='[[2bpd]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2bpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BPD FirstGlance]. <br> |
| - | [ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=2bpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpd OCA], [https://pdbe.org/2bpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bpd RCSB], [https://www.ebi.ac.uk/pdbsum/2bpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bpd ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/CLC7A_MOUSE CLC7A_MOUSE] Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation.<ref>PMID:10779524</ref> <ref>PMID:11544516</ref> <ref>PMID:12719479</ref> <ref>PMID:15213161</ref> <ref>PMID:15729357</ref> <ref>PMID:15731053</ref> <ref>PMID:15845454</ref> <ref>PMID:16825490</ref> |
| - | + | == 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/bp/2bpd_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=2bpd ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The murine molecule dectin-1 (known as the beta-glucan receptor in humans) is an immune cell surface receptor implicated in the immunological defense against fungal pathogens. Sequence analysis has indicated that the dectin-1 extracellular domain is a C-type lectin-like domain, and functional studies have established that it binds fungal beta-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 angstroms resolution structure in which a short soaked natural beta-glucan is trapped in the crystal lattice. In vitro characterization of dectin-1 in the presence of its natural ligand indicates higher-order complex formation between dectin-1 and beta-glucans. These combined structural and biophysical data considerably extend the current knowledge of dectin-1 structure and function, and suggest potential mechanisms of defense against fungal pathogens. | ||
| - | ' | + | Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function.,Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, Brown GD, Jones EY Protein Sci. 2007 Jun;16(6):1042-52. Epub 2007 May 1. PMID:17473009<ref>PMID:17473009</ref> |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2bpd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Brown GD]] | ||
| + | [[Category: Brown J]] | ||
| + | [[Category: Gilbert RJC]] | ||
| + | [[Category: Gordon S]] | ||
| + | [[Category: Jones EY]] | ||
| + | [[Category: Marshall ASJ]] | ||
| + | [[Category: O'Callaghan CA]] | ||
| + | [[Category: Siebold C]] | ||
Current revision
STRUCTURE OF MURINE DECTIN-1
| |||||||||||
Categories: Large Structures | Mus musculus | Brown GD | Brown J | Gilbert RJC | Gordon S | Jones EY | Marshall ASJ | O'Callaghan CA | Siebold C
