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1ov2
From Proteopedia
| 1ov2, 39 NMR models () | |||||||||
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| Gene: | LRPAP1 OR A2MRAP (Homo sapiens) | ||||||||
| Related: | 1op1 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Ensemble of the solution structures of domain one 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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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.
About this Structure
1ov2 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- 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
