Journal of Structural and Functional Genomics

, Volume 7, Issue 3, pp 131–138

The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family

  • Christian Köhler
  • Olav M. Andersen
  • Annette Diehl
  • Gerd Krause
  • Peter Schmieder
  • Hartmut Oschkinat
Original Paper

DOI: 10.1007/s10969-007-9016-5

Cite this article as:
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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Abstract

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.

Keywords

Boca Ferredoxin-like-fold LDLR-family MESD NMR-structure-determination WNT-signalling 

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Christian Köhler
    • 1
  • Olav M. Andersen
    • 2
  • Annette Diehl
    • 1
  • Gerd Krause
    • 1
  • Peter Schmieder
    • 1
  • Hartmut Oschkinat
    • 1
  1. 1.Department of NMR-Supported Structural BiologyLeibniz-Institut für Molekulare PharmakologieBerlinGermany
  2. 2.Department of Molecular Cardiovascular ResearchMax-Delbrueck-Center for Molecular MedicineBerlinGermany

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