1ov2

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==Ensemble of the solution structures of domain one of receptor associated protein==
==Ensemble of the solution structures of domain one of receptor associated protein==
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<StructureSection load='1ov2' size='340' side='right'caption='[[1ov2]], [[NMR_Ensembles_of_Models | 39 NMR models]]' scene=''>
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<StructureSection load='1ov2' size='340' side='right'caption='[[1ov2]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ov2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OV2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ov2]] 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=1OV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OV2 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1op1|1op1]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LRPAP1 OR A2MRAP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1ov2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ov2 OCA], [https://pdbe.org/1ov2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ov2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ov2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ov2 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=1ov2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ov2 OCA], [https://pdbe.org/1ov2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ov2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ov2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ov2 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
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[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.
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[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ov2 ConSurf].
</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=1ov2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.
 
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1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein.,Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX J Biomol NMR. 2003 Jun;26(2):187-8. PMID:12766414<ref>PMID:12766414</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 1ov2" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Migliorini, M]]
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[[Category: Migliorini M]]
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[[Category: Strickland, D K]]
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[[Category: Strickland DK]]
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[[Category: Wang, Y X]]
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[[Category: Wang YX]]
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[[Category: Wu, Y]]
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[[Category: Wu Y]]
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[[Category: Yu, P]]
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[[Category: Yu P]]
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[[Category: Helical protein]]
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[[Category: Receptor associated protein]]
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Revision as of 05:50, 17 April 2024

Ensemble of the solution structures of domain one of receptor associated protein

PDB ID 1ov2

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