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活性位点比较突出了肌球蛋白与其他P环蛋白之间的结构相似性。

Active site comparisons highlight structural similarities between myosin and other P-loop proteins.

作者信息

Smith C A, Rayment I

机构信息

Institute for Enzyme Research, University of Wisconsin, Madison 53705, USA.

出版信息

Biophys J. 1996 Apr;70(4):1590-602. doi: 10.1016/S0006-3495(96)79745-X.

Abstract

The phosphate binding loop (P-loop) is a common feature of a large number of enzymes that bind nucleotide whose consensus sequence is often used as a fingerprint for identifying new members of this group. We review here the binding sites of nine purine nucleotide binding proteins, with a focus on their relationship to the active site of myosin. This demonstrates that there is considerable conversation in the distribution and nature of the ligands that coordinate the triphosphate moiety. This comparison further suggests that at least myosin and the G-proteins utilize a similar mechanism for nucleotide hydrolysis.

摘要

磷酸结合环(P环)是大量结合核苷酸的酶的共同特征,其共有序列常被用作识别该类新成员的指纹。我们在此综述九种嘌呤核苷酸结合蛋白的结合位点,重点关注它们与肌球蛋白活性位点的关系。这表明在配位三磷酸部分的配体的分布和性质方面存在相当多的一致性。这种比较进一步表明,至少肌球蛋白和G蛋白利用相似的机制进行核苷酸水解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e73b/1225128/cda094d6cd97/biophysj00050-0025-a.jpg

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