A complete NMR spectral assignment of the conserved region of the MESD protein, MESD(12-155).
The low-density lipoprotein (LDL) receptor family members control diverse developmental and physiological pathways. Mesoderm development (MESD) protein is a 195-residue protein that functions as a specialized molecular chaperone to promote the proper folding of the six-bladed beta-propeller/EGF modules of the LDL receptor family members. Here we report a complete NMR spectral assignment of the most conserved region of MESD protein, MESD(12-155).
Chen
Jianglei
J
Department of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, Detroit, MI 48201, USA.
Bu
Guojun
G
Wang
Jianjun
J
D000818:Animals; D017124:Conserved Sequence; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011973:Receptors, LDL / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
C472170:MESD protein, mouse; D018832:Molecular Chaperones; D010446:Peptide Fragments; D011973:Receptors, LDL; D011994:Recombinant Proteins