1ov2 | pdb_00001ov2
From Proteopedia
Ensemble of the solution structures of domain one of receptor associated protein
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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 PubMedThe 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 | ||||||||||||||||||||
This page was last modified 08:26, 23 February 2022.