BINDING-SITES FOR CALCIUM, LIPID AND P11 ON P36, THE SUBSTRATE OF RETROVIRAL TYROSINE-SPECIFIC PROTEIN-KINASES
BINDING-SITES FOR CALCIUM, LIPID AND P11 ON P36, THE SUBSTRATE OF RETROVIRAL TYROSINE-SPECIFIC PROTEIN-KINASES
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DOI：
10.1016/0014-5793(86)80437-9
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发表时间：
1986-03-31
期刊：
影响因子：
3.5
通讯作者：
WEBER, K
中科院分区：
文献类型：
--
作者：
JOHNSSON, N;VANDEKERCKHOVE, J;WEBER, K
生物化学和部分序列数据揭示了p36的双结构域结构。氨基末端约30个残基的松散结构包含可磷酸化的酪氨酸和p11调节链的结合位点。下面的p33结构域保留了脂质结合位点以及影响单个色氨酸和一个酪氨酸的光谱特性的Ca2+位点。覆盖约25%的分子的组合序列数据将p36鉴定为独特的多肽。
Biochemical and partial sequence data reveal the two‐domain structure of p36. A loose structure of some 30 residues at the amino‐terminus contains the phosphorylatable tyrosine and the binding site for the p11 regulatory chain. The following p33 domain retains the lipid‐binding site as well as the Ca2+site which influences the spectral properties of the single tryptophan and one tyrosine. The combined sequence data covering about 25% of the molecule identify p36 as a unique polypeptide.