View source for 2i1p


==Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin==
<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].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2i1p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Bade-Noskova V]]
[[Category: Dancea F]]
[[Category: Kerjaschki D]]
[[Category: Luecke C]]
[[Category: Rueterjans H]]
[[Category: Shi M]]
[[Category: Wolf CA]]