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犰狳酰基辅酶A结合蛋白（ACBP）的结构：酰基辅酶A结合蛋白家族的新成员。

Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family.

作者信息

Costabel Marcelo D, Ermácora Mario R, Santomé José A, Alzari Pedro M, Guérin Diego M A

机构信息

Grupo de Biofísica, Departamento de Física, Universidad Nacional del Sur, Bahía Blanca, Argentina.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):958-61. doi: 10.1107/S1744309106038164. Epub 2006 Sep 30.

DOI:10.1107/S1744309106038164
PMID:17012783
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2225200/
Abstract

The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved. ACBP is a carrier for activated long-chain fatty acids and has been associated with many aspects of lipid metabolism. Its secondary structure is highly similar to that of the corresponding form of bovine ACBP and exhibits the unique flattened alpha-helical bundle (up-down-down-up) motif reported for animal, yeast and insect ACBPs. Conformational differences are located in loops and turns, although these structural differences do not suffice to account for features that could be related to the unusual biochemistry and lipid metabolism of the Harderian gland.

摘要

已解析出南美犰狳绒毛栉犰狳哈德氏腺脱辅基酰基辅酶A结合蛋白（ACBP）四方晶型的X射线结构。ACBP是活化长链脂肪酸的载体，与脂质代谢的多个方面相关。其二级结构与牛ACBP相应晶型的二级结构高度相似，并呈现出动物、酵母和昆虫ACBP所报道的独特扁平α-螺旋束（上-下-下-上）基序。构象差异位于环和转角处，尽管这些结构差异不足以解释可能与哈德氏腺异常生物化学和脂质代谢相关的特征。

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Acyl-CoA-binding protein in the armadillo Harderian gland: its primary structure and possible role in lipid secretion.
Biochim Biophys Acta. 2001 Feb 9;1545(1-2):314-25. doi: 10.1016/s0167-4838(00)00294-6.

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