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Band 3 function and dysfunction in a structural context

机译:结构背景下的3个功能和功能障碍

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Purpose of review Current research on the human band 3 glycoprotein, the red cell chloride/bicarbonate anion exchanger (AE1), is highlighted and placed within a structural context. Recent Findings The determination of the crystal structure of the membrane domain of human band 3, the founding member of the solute carrier 4 (SLC4) family of bicarbonate transporters, is a major breakthrough toward understanding the mechanism of action of this membrane transport protein, its interaction with partner proteins, and how mutations linked to disease affect its ability to fold and function. Summary Band 3 contains 14 transmembrane segments arranged in a 7+7 transmembrane inverted repeat topology common to all members of the SLC4 family and the unrelated SLC26 anion transporter family. A functional feature of this fold is the presence of a core and a gate domain: the core domain contains two short transmembrane helices (TM3 and 10) that face each other in the middle of the membrane with the positive N-terminal helix dipoles creating the anion-binding site, whereas the gate domain forms the dimer interface. During transport, the movement of these two domains relative to each other provides the intracellular and extracellular compartments with alternating access to the central anion-binding site.
机译:审查对人带3糖蛋白的目前研究的目的,突出显示并置于结构背景下的红细胞氯化物/碳酸酯阴离子交换器(AE1)。最近发现人带3的膜结构域的晶体结构的测定,溶质载体4(SLC4)的碳酸氢盐转运蛋白家族的创始构件是了解该膜输送蛋白的作用机制的重大突破与合作伙伴蛋白的相互作用,以及如何与疾病相关的突变会影响其折叠和功能的能力。汇总3包含14个跨膜段,布置在7 + 7个跨膜反复重复拓扑中,该段是SLC4家族的所有成员和不相关的SLC26阴离子运输家族的共同。该折叠的功能特征是存在核心和栅极域:核心结构域包含两个短的跨膜螺旋(TM3和10),其在膜的中间彼此面对,正面末端螺旋偶极偶联产生阴离子绑定站点,而栅极域形成二聚体界面。在运输过程中,这两个结构域相对于彼此的运动提供细胞内和细胞外隔室,其交替进入中心阴离子结合位点。

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