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2i1p
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2i1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i1p" /> '''Solution structure of the twelfth cysteine-r...) |
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| - | [[Image:2i1p.jpg|left|200px]]<br /><applet load="2i1p" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2i1p" /> | ||
| - | '''Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin'''<br /> | ||
| - | == | + | ==Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin== |
| - | Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as | + | <StructureSection load='2i1p' size='340' side='right'caption='[[2i1p]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2i1p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2i1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1p OCA], [https://pdbe.org/2i1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1p RCSB], [https://www.ebi.ac.uk/pdbsum/2i1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LRP2_RAT LRP2_RAT] Acts together with cubilin to mediate HDL endocytosis (By similarity). Receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B.<ref>PMID:7544804</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/2i1p_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2i1p ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence. | ||
| - | + | Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin.,Wolf CA, Dancea F, Shi M, Bade-Noskova V, Ruterjans H, Kerjaschki D, Lucke C J Biomol NMR. 2007 Apr;37(4):321-8. Epub 2007 Jan 24. PMID:17245526<ref>PMID:17245526</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2i1p" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | + | [[Category: Bade-Noskova V]] | |
| - | [[Category: Bade-Noskova | + | [[Category: Dancea F]] |
| - | [[Category: Dancea | + | [[Category: Kerjaschki D]] |
| - | [[Category: Kerjaschki | + | [[Category: Luecke C]] |
| - | [[Category: Luecke | + | [[Category: Rueterjans H]] |
| - | [[Category: Rueterjans | + | [[Category: Shi M]] |
| - | [[Category: Shi | + | [[Category: Wolf CA]] |
| - | [[Category: Wolf | + | |
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Current revision
Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin
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