2I1P
Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin
Summary for 2I1P
| Entry DOI | 10.2210/pdb2i1p/pdb |
| NMR Information | BMRB: 7263 |
| Descriptor | Low-density lipoprotein receptor-related protein 2, CALCIUM ION (2 entities in total) |
| Functional Keywords | low density lipoprotein receptor, cysteine-rich repeat, ligand binding domain, calcium cage, ligand binding protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 5137.70 |
| Authors | Wolf, C.A.,Dancea, F.,Shi, M.,Bade-Noskova, V.,Rueterjans, H.,Kerjaschki, D.,Luecke, C. (deposition date: 2006-08-14, release date: 2007-02-13, Last modification date: 2023-06-14) |
| Primary citation | Wolf, C.A.,Dancea, F.,Shi, M.,Bade-Noskova, V.,Rueterjans, H.,Kerjaschki, D.,Luecke, C. Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin. J.Biomol.Nmr, 37:321-328, 2007 Cited by PubMed Abstract: 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. PubMed: 17245526DOI: 10.1007/s10858-006-9129-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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