Lesk A M
University of Cambridge Clinical School, UK.
Curr Opin Struct Biol. 1995 Dec;5(6):775-83. doi: 10.1016/0959-440x(95)80010-7.
The nicotinamide adenine dinucleotide (NAD)-binding domains of dehydrogenases, containing a conserved double beta-alpha-beta-alpha-beta motif, are 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.
脱氢酶的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）及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中为这类分子创造天然结合位点的特征。该结构域继续以具有不同外围添加物或变体的共同核心形式出现在许多结构中。其他结合NAD及相关分子的结构使用完全不同的拓扑结构，不过，在许多结构中，磷酸基团出现在α螺旋的N端。铁氧化还原蛋白还原酶似乎显示出趋同进化，它含有一个单一的β-α-β基序，其结构及其与配体的相互作用与脱氢酶中的一个区域相似。
