2fyj

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{{Seed}}
 
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[[Image:2fyj.png|left|200px]]
 
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==NMR Solution structure of calcium-loaded LRP double module==
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The line below this paragraph, containing "STRUCTURE_2fyj", creates the "Structure Box" on the page.
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<StructureSection load='2fyj' size='340' side='right'caption='[[2fyj]]' 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'>[[2fyj]] 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=2FYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYJ 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, 15 models</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=2fyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyj OCA], [https://pdbe.org/2fyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyj RCSB], [https://www.ebi.ac.uk/pdbsum/2fyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyj ProSAT]</span></td></tr>
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{{STRUCTURE_2fyj| PDB=2fyj | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LRP1_HUMAN LRP1_HUMAN] Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.<ref>PMID:1702392</ref> <ref>PMID:1618748</ref> <ref>PMID:11907044</ref> <ref>PMID:12888553</ref> <ref>PMID:12713657</ref> Functions as a receptor for Pseudomonas aeruginosa exotoxin A.<ref>PMID:1702392</ref> <ref>PMID:1618748</ref> <ref>PMID:11907044</ref> <ref>PMID:12888553</ref> <ref>PMID:12713657</ref>
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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/fy/2fyj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fyj 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 low-density lipoprotein receptor-related protein (LRP) interacts with more than 30 ligands of different sizes and structures that can all be replaced by the receptor-associated protein (RAP). The double module of complement type repeats, CR56, of LRP binds many ligands including all three domains of RAP and alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease. To understand the receptor-ligand cross-talk, the NMR structure of CR56 has been solved and ligand binding experiments with RAP domain 1 (RAPd1) have been performed. From chemical shift perturbations of both binding partners upon complex formation, a HADDOCK model of the complex between CR56 and RAPd1 has been obtained. The binding residues are similar to a common binding motif suggested from alpha2-macroglobulin binding studies and provide evidence for an understanding of their mutual cross-competition pattern. The present structural results convey a simultaneous description of both binding partners of an LRP-ligand complex and open a route to a broader understanding of the binding specificity of the LRP receptor, which may involve a general four-residue receptor-ligand recognition motif common to all LRP ligands. The present result may be beneficial in the design of antagonists of ligand binding to the LDL receptor family, and especially of drugs for treatment of Alzheimer's disease.
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===NMR Solution structure of calcium-loaded LRP double module===
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Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif.,Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thogersen HC, O'Shea C, Poulsen FM, Kragelund BB J Mol Biol. 2006 Sep 29;362(4):700-16. Epub 2006 Jul 15. PMID:16938309<ref>PMID:16938309</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_16938309}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fyj" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16938309 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16938309}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2FYJ is a [[Single protein]] 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=2FYJ OCA].
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==Reference==
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Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif., Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thogersen HC, O'Shea C, Poulsen FM, Kragelund BB, J Mol Biol. 2006 Sep 29;362(4):700-16. Epub 2006 Jul 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16938309 16938309]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9207124 9207124]
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Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP., Andersen OM, Christensen LL, Christensen PA, Sorensen ES, Jacobsen C, Moestrup SK, Etzerodt M, Thogersen HC, J Biol Chem. 2000 Jul 14;275(28):21017-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747921 10747921]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Andersen, O M.]]
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[[Category: Andersen OM]]
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[[Category: Bjerrum-Bohr, I.]]
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[[Category: Bjerrum-Bohr I]]
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[[Category: Bonvin, A M.]]
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[[Category: Bonvin AM]]
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[[Category: Etzerodt, M.]]
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[[Category: Etzerodt M]]
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[[Category: Jensen, G A.]]
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[[Category: Jensen GA]]
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[[Category: Kragelund, B B.]]
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[[Category: Kragelund BB]]
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[[Category: Poulsen, F M.]]
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[[Category: O'shea C]]
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[[Category: Shea, C O.]]
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[[Category: Poulsen FM]]
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[[Category: Beta-2 hairpin]]
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[[Category: Calcium]]
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[[Category: Complement type repeat]]
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[[Category: Double module]]
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[[Category: Loop-structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:40:19 2008''
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Current revision

NMR Solution structure of calcium-loaded LRP double module

PDB ID 2fyj

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