Molecular basis for insulin fibril assembly Export

@article{Ivanova2009, abstract = {10.1073/pnas.0910080106 In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio\^{a}€“dependent manner, suggesting that this segment is central to the cross-\^{I}² spine of the insulin fibril. In isolation from the rest of the protein, LVEALYL forms microcrystalline aggregates with fibrillar morphology, the structure of which we determined to 1 \~{A}… resolution. The LVEALYL segments are stacked into pairs of tightly interdigitated \^{I}²-sheets, each pair displaying the dry steric zipper interface typical of amyloid-like fibrils. This structure leads to a model for fibrils of human insulin consistent with electron microscopic, x-ray fiber diffraction, and biochemical studies.}, author = {Ivanova, Magdalena I. and Sievers, Stuart A. and Sawaya, Michael R. and Wall, Joseph S. and Eisenberg, David}, citeulike-article-id = {6058711}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0910080106}, citeulike-linkout-1 = {http://www.pnas.org/content/0910080106v1/.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/0910080106v1/.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19864624}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19864624}, day = {28}, doi = {10.1073/pnas.0910080106}, journal = {Proceedings of the National Academy of Sciences}, keywords = {amyloid, xrd}, month = {October}, posted-at = {2009-11-03 09:37:34}, priority = {2}, title = {Molecular basis for insulin fibril assembly}, url = {http://dx.doi.org/10.1073/pnas.0910080106}, year = {2009} }

TY - JOUR ID - Ivanova2009 L3 - citeulike-article-id:6058711 N2 - 10.1073/pnas.0910080106 In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio–dependent manner, suggesting that this segment is central to the cross-β spine of the insulin fibril. In isolation from the rest of the protein, LVEALYL forms microcrystalline aggregates with fibrillar morphology, the structure of which we determined to 1 Å resolution. The LVEALYL segments are stacked into pairs of tightly interdigitated β-sheets, each pair displaying the dry steric zipper interface typical of amyloid-like fibrils. This structure leads to a model for fibrils of human insulin consistent with electron microscopic, x-ray fiber diffraction, and biochemical studies. JF - Proceedings of the National Academy of Sciences TI - Molecular basis for insulin fibril assembly KW - amyloid KW - xrd AU - Ivanova, Magdalena AU - Sievers, Stuart AU - Sawaya, Michael AU - Wall, Joseph AU - Eisenberg, David PY - 2009/10/28/ UR - http://dx.doi.org/10.1073/pnas.0910080106 ER -