Kini R M, Evans H J
Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298-0614, USA.
Biochem Biophys Res Commun. 1995 Jul 26;212(3):1115-24. doi: 10.1006/bbrc.1995.2084.
An examination of more than 1600 protein-protein interaction sites indicated that proline is the residue most commonly found near interaction sites. A structural role is distinguished for these proline residues in the flanking segments of protein-protein interaction sites. The unique nature of proline helps protect the integrity and present the sites, thus promoting protein-protein interactions. A novel approach to the design and development of potent peptide drugs and a simple predictive method to identify protein-protein interaction sites directly from the amino acid sequence have been developed based on this finding. The recognition of this structural role for proline has strong implications for protein chemistry and protein engineering.
对1600多个蛋白质-蛋白质相互作用位点的研究表明，脯氨酸是在相互作用位点附近最常见的残基。在蛋白质-蛋白质相互作用位点侧翼区域的这些脯氨酸残基具有独特的结构作用。脯氨酸的独特性质有助于保护其完整性并呈现这些位点，从而促进蛋白质-蛋白质相互作用。基于这一发现，已经开发出一种设计和开发强效肽药物的新方法以及一种直接从氨基酸序列识别蛋白质-蛋白质相互作用位点的简单预测方法。对脯氨酸这一结构作用的认识对蛋白质化学和蛋白质工程具有重要意义。
