Structural highlights2li9 is a 2 chain structure. Full experimental information is available from OCA. Publication Abstract from PubMedIn 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 beta-amyloid (rat Abeta(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 Abeta(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Abeta dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat Abeta(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. NMR solution structure of rat abeta(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease.,Istrate AN, Tsvetkov PO, Mantsyzov AB, Kulikova AA, Kozin SA, Makarov AA, Polshakov VI Biophys J. 2012 Jan 4;102(1):136-43. Epub 2012 Jan 3. PMID:22225807[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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