1OV2

Ensemble of the solution structures of domain one of receptor associated protein

Summary for 1OV2

• Entry DOI: 10.2210/pdb1ov2/pdb
• Related: 1op1
• NMR Information: BMRB: 5598
• Descriptor: Alpha-2-macroglobulin receptor-associated protein precursor (1 entity in total)
• Functional Keywords: helical protein, receptor associated protein
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum: P30533
• Total number of polymer chains: 1
• Total formula weight: 11681.40

Authors

Wu, Y.,Migliorini, M.,Yu, P.,Strickland, D.K.,Wang, Y.X. (deposition date: 2003-03-25, release date: 2004-04-06, Last modification date: 2024-05-22)

Primary citation

Wu, Y.,Migliorini, M.,Yu, P.,Strickland, D.K.,Wang, Y.X.
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein.
J.Biomol.Nmr, 26:187-188, 2003

PubMed 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 (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.

PubMed: 12766414
DOI: 10.1023/A:1023534107920

Experimental method

SOLUTION NMR