2i9s: Difference between revisions

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[[Image:2i9s.jpg|left|200px]]


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==The solution structure of the core of mesoderm development (MESD).==
The line below this paragraph, containing "STRUCTURE_2i9s", creates the "Structure Box" on the page.
<StructureSection load='2i9s' size='340' side='right'caption='[[2i9s]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2i9s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I9S FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=2i9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i9s OCA], [https://pdbe.org/2i9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i9s RCSB], [https://www.ebi.ac.uk/pdbsum/2i9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i9s ProSAT]</span></td></tr>
{{STRUCTURE_2i9s| PDB=2i9s  | SCENE= }}
</table>
 
== Function ==
'''The solution structure of the core of mesoderm development (MESD).'''
[https://www.uniprot.org/uniprot/MESD_MOUSE MESD_MOUSE] Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction.<ref>PMID:12581525</ref> <ref>PMID:21397183</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/2i9s_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=2i9s ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mesoderm development (MESD) is a 224 amino acid mouse protein that acts as a molecular chaperone for receptors of the low-density lipoprotein receptor (LDLR) family. By recording (15)N-HSQC-NMR spectra of six different MESD constructs, we could determine a highly structured core region corresponding to residues 104-177. Here we firstly present the solution structure of this highly conserved core of MESD. It shows a four-stranded anti-parallel beta-sheet and two alpha-helices situated on one side of the sheet. Although described in the literature as structurally homologues to ferredoxins, the connectivity of secondary structure elements is different in the MESD fold. A structural comparison to entries of the PDB reveals a frequent domain with low sequence homology annotated as HMA and P-II domains in Pfam.
Mesoderm development (MESD) is a 224 amino acid mouse protein that acts as a molecular chaperone for receptors of the low-density lipoprotein receptor (LDLR) family. By recording (15)N-HSQC-NMR spectra of six different MESD constructs, we could determine a highly structured core region corresponding to residues 104-177. Here we firstly present the solution structure of this highly conserved core of MESD. It shows a four-stranded anti-parallel beta-sheet and two alpha-helices situated on one side of the sheet. Although described in the literature as structurally homologues to ferredoxins, the connectivity of secondary structure elements is different in the MESD fold. A structural comparison to entries of the PDB reveals a frequent domain with low sequence homology annotated as HMA and P-II domains in Pfam.


==About this Structure==
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.,Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:17342452<ref>PMID:17342452</ref>
2I9S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I9S OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family., Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H, J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17342452 17342452]
</div>
<div class="pdbe-citations 2i9s" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Andersen O]]
[[Category: Andersen, O.]]
[[Category: Diehl A]]
[[Category: Diehl, A.]]
[[Category: Koehler C]]
[[Category: Koehler, C.]]
[[Category: Krause G]]
[[Category: Krause, G.]]
[[Category: Oschkinat H]]
[[Category: Oschkinat, H.]]
[[Category: Schmieder P]]
[[Category: Schmieder, P.]]
[[Category: Ferredoxin-like-fold]]
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Retrieved from "https://proteopedia.org/2i9s"