1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein.
The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.
Wu
YiBing
Y
Migliorini
Molly
M
Yu
Ping
P
Strickland
Dudely K
DK
Wang
Yun-Xing
YX
D000595:Amino Acid Sequence; D024322:Amino Acids, Aromatic; D000818:Animals; D002247:Carbon Isotopes; D026563:LDL-Receptor Related Protein-Associated Protein / Q000737:chemistry*; D051379:Mice; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011522:Protons
D024322:Amino Acids, Aromatic; D002247:Carbon Isotopes; D026563:LDL-Receptor Related Protein-Associated Protein; D009587:Nitrogen Isotopes; D011522:Protons