1lre

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{{Seed}}
 
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[[Image:1lre.png|left|200px]]
 
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==RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1lre", creates the "Structure Box" on the page.
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<StructureSection load='1lre' size='340' side='right'caption='[[1lre]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1lre]] 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=1LRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LRE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lre OCA], [https://pdbe.org/1lre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lre RCSB], [https://www.ebi.ac.uk/pdbsum/1lre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lre ProSAT]</span></td></tr>
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{{STRUCTURE_1lre| PDB=1lre | SCENE= }}
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</table>
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== 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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== 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/1lre_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1lre ConSurf].
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<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 three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain.
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===RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES===
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The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.,Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7521-5. PMID:9207124<ref>PMID:9207124</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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The line below this paragraph, {{ABSTRACT_PUBMED_9207124}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1lre" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9207124 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9207124}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1LRE is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LRE OCA].
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==Reference==
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<ref group="xtra">PMID:9207124</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nielsen, P R.]]
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[[Category: Large Structures]]
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[[Category: Poulsen, F M.]]
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[[Category: Nielsen PR]]
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[[Category: Alpha2-macroglobulin receptor associated protein]]
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[[Category: Poulsen FM]]
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[[Category: Helix bundle]]
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[[Category: Ldlr family associated protein]]
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[[Category: Low density lipoprotein receptor family associated protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:22:00 2009''
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Current revision

RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES

PDB ID 1lre

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