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2i9s

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|ACTIVITY=
|ACTIVITY=
|GENE= Mesdc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= Mesdc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i9s OCA], [http://www.ebi.ac.uk/pdbsum/2i9s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i9s RCSB]</span>
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[[Category: ferredoxin-like-fold]]
[[Category: ferredoxin-like-fold]]
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Revision as of 00:41, 31 March 2008


PDB ID 2i9s

Drag the structure with the mouse to rotate
Gene: Mesdc2 (Mus musculus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The solution structure of the core of mesoderm development (MESD).


Overview

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

2I9S is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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