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1
Determination of the gelsolin binding site on F-actin: implications for severing and capping.凝溶胶蛋白在F-肌动蛋白上结合位点的确定：对切割和封端的影响。
Biophys J. 1998 Feb;74(2 Pt 1):764-72. doi: 10.1016/S0006-3495(98)74001-9.
2
Characterization of gelsolin truncates that inhibit actin depolymerization by severing activity of gelsolin and cofilin.凝溶胶蛋白截短体的特性研究，这些截短体通过凝溶胶蛋白和丝切蛋白的切断活性来抑制肌动蛋白解聚。
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3
Molecular model of an actin filament capped by a severing protein.由一种切割蛋白封端的肌动蛋白丝的分子模型。
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4
The actin side-binding domain of gelsolin also caps actin filaments. Implications for actin filament severing.凝溶胶蛋白的肌动蛋白侧结合结构域也会封闭肌动蛋白丝。对肌动蛋白丝切断的影响。
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5
The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence.在存在钙离子的情况下，绒毛蛋白的分离出的第六个凝溶胶蛋白重复序列和头部结构域可将F-肌动蛋白成束，并且它们由一段40个残基的无结构序列相连。
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Probing the effects of calcium on gelsolin.探究钙对凝溶胶蛋白的影响。
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Exome sequencing establishes a gelsolin mutation as the cause of inherited bulbar-onset neuropathy.外显子组测序确定凝溶胶蛋白突变是遗传性延髓起病神经病的病因。
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本文引用的文献

1
Inhibition of apoptosis by the actin-regulatory protein gelsolin.肌动蛋白调节蛋白凝溶胶蛋白对细胞凋亡的抑制作用。
EMBO J. 1997 Aug 1;16(15):4650-6. doi: 10.1093/emboj/16.15.4650.
2
Delayed retraction of filopodia in gelsolin null mice.凝溶胶蛋白基因敲除小鼠中丝状伪足的延迟回缩。
J Cell Biol. 1997 Sep 22;138(6):1279-87. doi: 10.1083/jcb.138.6.1279.
3
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.血浆凝溶胶蛋白的晶体结构：对肌动蛋白切断、加帽和成核的影响。
Cell. 1997 Aug 22;90(4):661-70. doi: 10.1016/s0092-8674(00)80527-9.
4
Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function.丝切蛋白改变F-肌动蛋白的螺旋：对肌动蛋白丝动力学和细胞功能的影响。
J Cell Biol. 1997 Aug 25;138(4):771-81. doi: 10.1083/jcb.138.4.771.
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Conformational changes in actin induced by its interaction with gelsolin.肌动蛋白与凝溶胶蛋白相互作用诱导的构象变化。
Biophys J. 1997 Aug;73(2):929-37. doi: 10.1016/S0006-3495(97)78125-6.
6
Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon.重组平滑肌细肌丝的三维图像重建：钙调蛋白的作用。
Biophys J. 1997 Jun;72(6):2398-404. doi: 10.1016/S0006-3495(97)78885-4.
7
Kinetics of gelsolin interaction with phalloidin-stabilized F-actin. Rate constants for binding and severing.凝溶胶蛋白与鬼笔环肽稳定的F-肌动蛋白相互作用的动力学。结合和解聚的速率常数。
Biochemistry. 1996 Dec 24;35(51):16550-6. doi: 10.1021/bi961891j.
8
Actin filaments mediate DNA fiber formation in chronic inflammatory airway disease.肌动蛋白丝在慢性炎症性气道疾病中介导DNA纤维形成。
Am J Pathol. 1996 Mar;148(3):919-27.
9
CTF determination of images of ice-embedded single particles using a graphics interface.使用图形界面通过计算机断层扫描荧光法测定冰包埋单颗粒的图像
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SUPRIM: easily modified image processing software.SUPRIM：易于修改的图像处理软件。
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凝溶胶蛋白在F-肌动蛋白上结合位点的确定：对切割和封端的影响。

Determination of the gelsolin binding site on F-actin: implications for severing and capping.

作者信息

McGough A, Chiu W, Way M

机构信息

Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA.

出版信息

Biophys J. 1998 Feb;74(2 Pt 1):764-72. doi: 10.1016/S0006-3495(98)74001-9.

DOI:10.1016/S0006-3495(98)74001-9
PMID:9533689
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1302557/
Abstract

Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes.

摘要

凝溶胶蛋白是一种六结构域蛋白，通过切断、封端和成核细丝来调节肌动蛋白组装。我们利用电子冷冻显微镜和螺旋重建技术来确定其在F-肌动蛋白上的结合位点。为了在切断条件下获得完全修饰的细丝，我们研究了一种与凝溶胶蛋白相比切断效率降低的衍生物（G2-6）。通过电子冷冻显微镜和螺旋重建技术获得了G2-6:F-肌动蛋白的三维重建结构。该结构表明，凝溶胶蛋白结合细丝时会桥接两个纵向相关的单体。G2-6的F-肌动蛋白结合区域轴向位于上部肌动蛋白单体亚结构域3的中心，径向位于亚结构域1和3之间。我们的结果表明，为了发生切断，凝溶胶蛋白和肌动蛋白都会发生大的构象变化。