NAD-binding domains of dehydrogenases
NAD-binding domains of dehydrogenases
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DOI：
10.1016/0959-440x(95)80010-7
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发表时间：
1995-12-01
影响因子：
6.8
通讯作者：
Lesk, AM
中科院分区：
文献类型：
--
作者：
Lesk, AM
烟酰胺腺嘌呤二核苷酸（NAD）结合结构域包含保守的双β-α-β-α-β基序，是许多结合NAD、烟酰胺腺嘌呤二核苷酸磷酸（NADP）和相关辅因子的酶的共同结构特征。已经描述了这种折叠模式的特征，其为这些分子产生天然结合位点。域继续出现在许多结构中，以具有不同外围添加或变化的共同核心的形式。结合NAD和相关分子的其他结构使用完全不同的拓扑结构，尽管在许多情况下，磷酸基团出现在α螺旋的N末端。铁氧还蛋白还原酶似乎显示出趋同进化，包含一个单一的β-α-β基序，该基序在结构和与酶中某个区域的配体的相互作用方面都相似。
The nicotinamide adenine dinucleotide (NAD)-binding domains of dehydrogenases, containing a conserved double beta-alpha-beta-alpha-beta motif, are a common structural feature of many enzymes that bind NAD, nicotinamide adenine dinucleotide phosphate (NADP) and related cofactors. Features of this folding pattern that create a natural binding site for such molecules have been described. The domain continues to appear in many structures, in the form of a common core with different peripheral additions or variations. Other structures that bind NAD and related molecules use entirely different topologies, although, in many, a phosphate group appears at the N terminus of an alpha helix. Ferredoxin reductase seems to show convergent evolution, containing a single beta-alpha-beta motif that is similar both in its structure and in its interactions with the ligand to a region in dehydrogenases.