2i9s | pdb_00002i9s
The solution structure of the core of mesoderm development (MESD).
Structural highlights
FunctionMESD_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.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMesoderm 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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