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==Solution structure of the water-soluble LU-domain of human Lypd6 protein==
==Solution structure of the water-soluble LU-domain of human Lypd6 protein==
<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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[6ib6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6IB6 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ib6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ib6 OCA], [https://pdbe.org/6ib6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ib6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ib6 PDBsum], [https://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>
[https://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kulbatskii, D S]]
[[Category: Kulbatskii DS]]
[[Category: Lyukmanova, E N]]
[[Category: Lyukmanova EN]]
[[Category: Paramonov, A S]]
[[Category: Paramonov AS]]
[[Category: Shenkarev, Z O]]
[[Category: Shenkarev ZO]]
[[Category: Tsarev, A V]]
[[Category: Tsarev AV]]
[[Category: Ly6/upar]]
[[Category: Lypd6]]
[[Category: Neuropeptide]]
[[Category: Nicotinic acetylcholine receptor]]
[[Category: Signaling protein]]
[[Category: Three-finger protein]]

Latest revision as of 13:03, 23 October 2024

Solution structure of the water-soluble LU-domain of human Lypd6 proteinSolution structure of the water-soluble LU-domain of human Lypd6 protein

Structural highlights

6ib6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][1]

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.

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Arvaniti M, Jensen MM, Soni N, Wang H, Klein AB, Thiriet N, Pinborg LH, Muldoon PP, Wienecke J, Imad Damaj M, Kohlmeier KA, Gondre-Lewis MC, Mikkelsen JD, Thomsen MS. Functional interaction between Lypd6 and nicotinic acetylcholine receptors. J Neurochem. 2016 Sep;138(6):806-20. doi: 10.1111/jnc.13718. Epub 2016 Aug 15. PMID:27344019 doi:http://dx.doi.org/10.1111/jnc.13718
  2. ↑ Paramonov AS, Kocharovskaya MV, Tsarev AV, Kulbatskii DS, Loktyushov EV, Shulepko MA, Kirpichnikov MP, Lyukmanova EN, Shenkarev ZO. Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors. Int J Mol Sci. 2020 Oct 1;21(19). pii: ijms21197280. doi: 10.3390/ijms21197280. PMID:33019770 doi:http://dx.doi.org/10.3390/ijms21197280
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