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膜联蛋白A8的晶体结构与膜联蛋白A3的晶体结构相似。

The crystal structure of annexin A8 is similar to that of annexin A3.

作者信息

Réty Stéphane, Sopková-de Oliveira Santos Jana, Dreyfuss Lise, Blondeau Karine, Hofbauerová Katerina, Raguénès-Nicol Céline, Kerboeuf Daniel, Renouard Madalena, Russo-Marie Françoise, Lewit-Bentley Anita

机构信息

LURE, Centre Universitaire Paris-Sud, BP 34, 91898 Orsay Cedex, France.

出版信息

J Mol Biol. 2005 Feb 4;345(5):1131-9. doi: 10.1016/j.jmb.2004.11.015. Epub 2004 Dec 8.

Abstract

Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship.

摘要

膜联蛋白A8是这个钙结合和膜结合蛋白大家族中相对罕见且研究较少的成员。然而,它与一种特定疾病——急性早幼粒细胞白血病有关。我们已经解析了它的三维结构,该结构包括一个适度长且完整的N端。该结构与膜联蛋白A3的结构最为接近,并突出了膜联蛋白分子中几个固有的柔性重要区域。N端类似于膜联蛋白A3的N端,因为它沿着分子的凹面排列,并部分插入其中心的亲水通道。由于膜联蛋白A3和A8在早幼粒细胞分化过程中均有表达,它们结构上的相似性可能暗示了一种功能关系。

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