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

Item Type:	Article
Title:	The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family
Creators Name:	Koehler, C. and Andersen, O.M. and Diehl, A. and Krause, G. and Schmieder, P. and Oschkinat, H.
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 (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.
Keywords:	Boca, Ferredoxin-Like-Fold, LDLR-Family, MESD, NMR-Structure-Determination, WNT-Signalling, Animals, Cattle, Mice, Rats
Source:	Journal of Structural and Functional Genomics
ISSN:	1345-711X
Publisher:	Kluwer Academic Publishers
Volume:	7
Number:	3-4
Page Range:	131-138
Date:	December 2006
Official Publication:	https://doi.org/10.1007/s10969-007-9016-5
PubMed:	View item in PubMed

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