Structural highlights
Function
[LRP2_RAT] Acts together with cubilin to mediate HDL endocytosis (By similarity). Receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B.[1]
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
Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.
Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin.,Wolf CA, Dancea F, Shi M, Bade-Noskova V, Ruterjans H, Kerjaschki D, Lucke C J Biomol NMR. 2007 Apr;37(4):321-8. Epub 2007 Jan 24. PMID:17245526[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Moestrup SK, Cui S, Vorum H, Bregengard C, Bjorn SE, Norris K, Gliemann J, Christensen EI. Evidence that epithelial glycoprotein 330/megalin mediates uptake of polybasic drugs. J Clin Invest. 1995 Sep;96(3):1404-13. PMID:7544804 doi:http://dx.doi.org/10.1172/JCI118176
- ↑ Wolf CA, Dancea F, Shi M, Bade-Noskova V, Ruterjans H, Kerjaschki D, Lucke C. Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin. J Biomol NMR. 2007 Apr;37(4):321-8. Epub 2007 Jan 24. PMID:17245526 doi:10.1007/s10858-006-9129-3
