1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein |
| |
| Authors: | Wu YiBing Migliorini Molly Yu Ping Strickland Dudely K Wang Yun-Xing |
| |
| Institution: | (1) Protein-Nucleic Acid NMR Section, Structural Biophysics Laboratory, National Cancer Institute (Frederick), National Institutes of Health, Frederick, MD, 21702, U.S.A;(2) Department of Vascular Biology, Jerome H. Holland Laboratory for Biomedical Science, American Red Cross, Rockville, MD, 20855, U.S.A |
| |
| Abstract: | 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 1H, 13C and 15N chemical shift signals of domain 1 of the RAP. |
| |
| Keywords: | domain 1 RAP receptor associated protein |
| 本文献已被 PubMed SpringerLink 等数据库收录！ |
|
