THE HELIX CLAMP IN HIV-1 REVERSE-TRANSCRIPTASE - A NEW NUCLEIC-ACID BINDING MOTIF COMMON IN NUCLEIC-ACID POLYMERASES
THE HELIX CLAMP IN HIV-1 REVERSE-TRANSCRIPTASE - A NEW NUCLEIC-ACID BINDING MOTIF COMMON IN NUCLEIC-ACID POLYMERASES
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DOI：
10.1093/nar/22.22.4625
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发表时间：
1994-11-11
影响因子：
14.9
通讯作者：
HEUMANN, H
中科院分区：
文献类型：
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作者：
HERMANN, T;MEIER, T;HEUMANN, H
与人类免疫缺陷病毒1型逆转录酶（HIV-1 RT）的（259）KLVGKL（X）（16）KLLR（284）同源的氨基酸序列在几种核苷酸聚合酶中是保守的。该氨基酸基序已在晶体结构模型中被鉴定为酶的核酸结合装置的元件。它是HIV-1 RT的“拇指”区域内的螺旋-转角-螺旋结构α H -转角-α l的一部分。该基序在一侧抓住复合的核酸。对HIV-1 RT与核酸片段复合物的分子模拟研究表明，该基序在p66亚基和p51亚基中具有结合功能，充当一种“螺旋夹”。鉴于其在核酸聚合酶中的广泛分布，螺旋夹基序被认为是对核酸结合具有普遍意义的结构。
Amino acid sequences homologous to (259)KLVGKL (X)(16) KLLR(284) of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) are conserved in several nucleotide polymerizing enzymes. This amino acid motif has been identified in the crystal structure model as an element of the enzyme's nucleic acid binding apparatus. It is part of the helix - turn - helix structure, alpha H - turn - alpha l, within the 'thumb' region of HIV-1 RT. The motif grasps the complexed nucleic acid at one side. Molecular modeling studies on HIV-1 RT in complex with a nucleic acid fragment suggest that the motif has binding function in the p66 subunit as well as in the p51 subunit, acting as a kind of 'helix clamp'. Given its wide distribution within the nucleic acid polymerases, the helix clamp motif is assumed to be a structure of general significance for nucleic acid binding.