3vlg

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[[Image:3vlg.jpg|left|200px]]
 
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==Crystal structure of the W150A mutant LOX-1 CTLD showing impaired OxLDL binding==
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The line below this paragraph, containing "STRUCTURE_3vlg", creates the "Structure Box" on the page.
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<StructureSection load='3vlg' size='340' side='right'caption='[[3vlg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3vlg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VLG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vlg OCA], [https://pdbe.org/3vlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vlg RCSB], [https://www.ebi.ac.uk/pdbsum/3vlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vlg ProSAT]</span></td></tr>
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{{STRUCTURE_3vlg| PDB=3vlg | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/OLR1_HUMAN OLR1_HUMAN] Note=Independent association genetic studies have implicated OLR1 gene variants in myocardial infarction susceptibility.<ref>PMID:12384789</ref> <ref>PMID:12807963</ref> <ref>PMID:15060104</ref> <ref>PMID:15276231</ref> <ref>PMID:15860461</ref> Note=OLR1 may be involved in Alzheimer disease (AD). Involvement in AD is however unclear: according to some authors (PubMed:12354387, PubMed:12810610 and PubMed:15976314), variations in OLR1 modify the risk of AD, while according to other (PubMed:15000751 and PubMed:15060104) they do not.<ref>PMID:12384789</ref> <ref>PMID:12807963</ref> <ref>PMID:15060104</ref> <ref>PMID:15276231</ref> <ref>PMID:15860461</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/OLR1_HUMAN OLR1_HUMAN] Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria.<ref>PMID:9052782</ref> <ref>PMID:11821063</ref> <ref>PMID:12354387</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lectin-like oxidized lipoprotein (OxLDL) receptor 1, LOX-1, is the major OxLDL receptor expressed on vascular endothelial cells. We have previously reported the ligand-recognition mode of LOX-1 based on the crystal structure of the ligand binding domain (C-type lectin-like domain, CTLD) and surface plasmon resonance analysis, which suggested that the functional significance of the CTLD dimer (the 'canonical' dimer) is to harbor the characteristic "basic spine" on its surface. In this study, we have identified the key inter-domain interactions in retaining the canonical CTLD dimer by X-ray structural analysis of the inactive mutant W150A CTLD. The canonical CTLD dimer forms through tight hydrophobic interactions, in which W150 engages in a lock-and-key manner and represents the main interaction. The loss of the Trp ring by mutation to Ala prevents the formation of the canonical dimer, as elucidated from docking calculations using the crystal structure of W150A CTLD. The results emphasize that the canonically formed CTLD dimer is essential for LOX-1 to bind to OxLDL, which supports our proposed view that the basic spine surface present in the correctly formed dimer plays a primal role in OxLDL recognition. This concept provides insight into the pathogenic pattern recognized by LOX-1 as a member of the pattern recognition receptors.
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===Crystal structure of the W150A mutant LOX-1 CTLD showing impaired OxLDL binding===
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Structural implication for the impaired binding of W150A mutant LOX-1 to oxidized low density lipoprotein, OxLDL.,Nakano S, Sugihara M, Yamada R, Katayanagi K, Tate SI Biochim Biophys Acta. 2012 Feb 18;1824(5):739-749. PMID:22369967<ref>PMID:22369967</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vlg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[LDL receptor|LDL receptor]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22369967 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22369967}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3vlg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLG OCA].
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==Reference==
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<ref group="xtra">PMID:022369967</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Katayanagi, K.]]
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[[Category: Large Structures]]
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[[Category: Nakano, S.]]
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[[Category: Katayanagi K]]
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[[Category: Sugihara, M.]]
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[[Category: Nakano S]]
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[[Category: Tate, S.]]
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[[Category: Sugihara M]]
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[[Category: Yamada, R.]]
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[[Category: Tate S]]
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[[Category: C-type lectin-like domain]]
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[[Category: Yamada R]]
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[[Category: Lipid binding protein]]
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[[Category: Membrane protein]]
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[[Category: Oxidized ldl receptor]]
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Current revision

Crystal structure of the W150A mutant LOX-1 CTLD showing impaired OxLDL binding

PDB ID 3vlg

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