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胰岛淀粉样多肽(胰淀素)交叉β链的原子结构。

Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).

作者信息

Wiltzius Jed J W, Sievers Stuart A, Sawaya Michael R, Cascio Duilio, Popov Dmitriy, Riekel Christian, Eisenberg David

机构信息

Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California 90095-1570, USA.

出版信息

Protein Sci. 2008 Sep;17(9):1467-74. doi: 10.1110/ps.036509.108. Epub 2008 Jun 12.

Abstract

Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full-length IAPP polymorph.

摘要

人胰岛淀粉样多肽(IAPP或胰淀素)是一种由37个氨基酸残基组成的激素,在几乎所有II型糖尿病患者的胰腺提取物中都发现有纤维状沉积物。尽管IAPP的细胞毒性已得到证实,但这些沉积物中发现的纤维状形式的结构尚不清楚。在这里,我们使IAPP的两个片段结晶,这两个片段自身会形成淀粉样纤维。确定了这两个片段NNFGAIL和SSTNVG的原子结构,并以此为基础建立了最常见的全长IAPP多晶型物的模型。

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