2LI9
Metal binding domain of rat beta-amyloid
Summary for 2LI9
| Entry DOI | 10.2210/pdb2li9/pdb |
| Related | 1ZE7 |
| NMR Information | BMRB: 17884 |
| Descriptor | Amyloid beta A4 protein, ZINC ION (2 entities in total) |
| Functional Keywords | alzheimer's disease, dimer formation, zinc binding, cell adhesion |
| Biological source | Rattus norvegicus (brown rat,rat,rats) |
| Cellular location | Membrane; Single-pass type I membrane protein: P08592 |
| Total number of polymer chains | 2 |
| Total formula weight | 3839.41 |
| Authors | Polshakov, V.,Istrate, A.,Kozin, S.,Makarov, A. (deposition date: 2011-08-25, release date: 2012-01-18, Last modification date: 2024-10-30) |
| Primary citation | Istrate, A.N.,Tsvetkov, P.O.,Mantsyzov, A.B.,Kulikova, A.A.,Kozin, S.A.,Makarov, A.A.,Polshakov, V.I. NMR solution structure of rat Abeta(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease. Biophys.J., 102:136-143, 2012 Cited by PubMed Abstract: In an attempt to reveal the mechanism of rats' resistance to Alzheimer's disease, we determined the structure of the metal-binding domain 1-16 of rat β-amyloid (rat Aβ(1-16)) in solution in the absence and presence of zinc ions. A zinc-induced dimerization of the domain was detected. The zinc coordination site was found to involve residues His-6 and His-14 of both peptide chains. We used experimental restraints obtained from analyses of NMR and isothermal titration calorimetry data to perform structure calculations. The calculations employed an explicit water environment and a simulated annealing molecular-dynamics protocol followed by quantum-mechanical/molecular-mechanical optimization. We found that the C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat Aβ(1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease. PubMed: 22225807DOI: 10.1016/j.bpj.2011.11.4006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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