Structural highlights
Disease
AMRP_HUMAN Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
Function
AMRP_HUMAN Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein.,Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX J Biomol NMR. 2003 Jun;26(2):187-8. PMID:12766414[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu Y, Migliorini M, Yu P, Strickland DK, Wang YX. 1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein. J Biomol NMR. 2003 Jun;26(2):187-8. PMID:12766414
