The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family
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- Köhler, C., Andersen, O.M., Diehl, A. et al. J Struct Funct Genomics (2006) 7: 131. doi:10.1007/s10969-007-9016-5
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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 15N-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 β-sheet and two α-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.