6ib6
From Proteopedia
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<StructureSection load='6ib6' size='340' side='right'caption='[[6ib6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='6ib6' size='340' side='right'caption='[[6ib6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ib6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IB6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6ib6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IB6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6IB6 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYPD6, UNQ3023/PRO9821 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ib6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ib6 OCA], [http://pdbe.org/6ib6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ib6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ib6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ib6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/LYPD6_HUMAN LYPD6_HUMAN]] Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Inhibits nicotine-induced Ca(2+) influx through nAChRs (PubMed:27344019). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).[UniProtKB:Q66IA6]<ref>PMID:27344019</ref> | [[http://www.uniprot.org/uniprot/LYPD6_HUMAN LYPD6_HUMAN]] Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Inhibits nicotine-induced Ca(2+) influx through nAChRs (PubMed:27344019). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).[UniProtKB:Q66IA6]<ref>PMID:27344019</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ly-6/uPAR or three-finger proteins (TFPs) contain a disulfide-stabilized beta-structural core and three protruding loops (fingers). In mammals, TFPs have been found in epithelium and the nervous, endocrine, reproductive, and immune systems. Here, using heteronuclear NMR, we determined the three-dimensional (3D) structure and backbone dynamics of the epithelial secreted protein SLURP-1 and soluble domains of GPI-anchored TFPs from the brain (Lynx2, Lypd6, Lypd6b) acting on nicotinic acetylcholine receptors (nAChRs). Results were compared with the data about human TFPs Lynx1 and SLURP-2 and snake alpha-neurotoxins WTX and NTII. Two different topologies of the beta-structure were revealed: one large antiparallel beta-sheet in Lypd6 and Lypd6b, and two beta-sheets in other proteins. alpha-Helical segments were found in the loops I/III of Lynx2, Lypd6, and Lypd6b. Differences in the surface distribution of charged and hydrophobic groups indicated significant differences in a mode of TFPs/nAChR interactions. TFPs showed significant conformational plasticity: the loops were highly mobile at picosecond-nanosecond timescale, while the beta-structural regions demonstrated microsecond-millisecond motions. SLURP-1 had the largest plasticity and characterized by the unordered loops II/III and cis-trans isomerization of the Tyr39-Pro40 bond. In conclusion, plasticity could be an important feature of TFPs adapting their structures for optimal interaction with the different conformational states of nAChRs. | ||
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| + | Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors.,Paramonov AS, Kocharovskaya MV, Tsarev AV, Kulbatskii DS, Loktyushov EV, Shulepko MA, Kirpichnikov MP, Lyukmanova EN, Shenkarev ZO Int J Mol Sci. 2020 Oct 1;21(19). pii: ijms21197280. doi: 10.3390/ijms21197280. PMID:33019770<ref>PMID:33019770</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ib6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kulbatskii, D S]] | [[Category: Kulbatskii, D S]] | ||
Revision as of 05:58, 20 January 2021
Solution structure of the water-soluble LU-domain of human Lypd6 protein
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