The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.
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.
Köhler
Christian
C
Department of NMR-Supported Structural Biology, Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, 13125 Berlin, Germany.
Andersen
Olav M
OM
Diehl
Annette
A
Krause
Gerd
G
Schmieder
Peter
P
Oschkinat
Hartmut
H
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D051381:Rats; D011973:Receptors, LDL / Q000378:metabolism*
C506348:MESD protein, human; D018832:Molecular Chaperones; D011973:Receptors, LDL