NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
Chen
Jianglei
J
Department of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, Detroit, MI 48201, USA.
Li
Qianqian
Q
Liu
Chia-Chen
CC
Zhou
Pei
P
Zhou
Bei
B
Bu
Guojun
G
Wang
Jianjun
J
D000595:Amino Acid Sequence; D000818:Animals; D004330:Drosophila; D029721:Drosophila Proteins / Q000737:chemistry; D006801:Humans; D026502:LDL-Receptor Related Proteins / Q000737:chemistry / Q000378:metabolism*; D008239:Lysine / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017510:Protein Folding; D016415:Sequence Alignment; D055672:Static Electricity
D029721:Drosophila Proteins; D026502:LDL-Receptor Related Proteins; C472170:MESD protein, mouse; D018832:Molecular Chaperones; C472169:boca protein, Drosophila; D008239:Lysine