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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Macromolecular recognition in the Protein Data Bank
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Macromolecular recognition in the Protein Data Bank

机译：在蛋白质大分子识别数据银行

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摘要

Crystal structures deposited in the Protein Data Bank illustrate the diversity of biological macromolecular recognition: transient interactions in protein-protein and protein DNA complexes and permanent assemblies in homodimeric proteins. The geometric and physical chemical properties of the macromolecular interfaces that may govern the stability and specificity of recognition are explored in complexes and homodimers compared with crystal-packing interactions. It is found that crystal-packing interfaces are usually much smaller; they bury fewer atoms and are less tightly packed than in specific assemblies. Standard-size interfaces burying 1200-2000 angstrom(2) of protein surface occur in protease-inhibitor and antigen-antibody complexes that assemble with little or no conformation changes. Short-lived electron-transfer complexes have small interfaces; the larger size of the interfaces observed in complexes involved in signal transduction and homodimers correlates with the presence of conformation changes, often implicated in biological function. Results of the CAPRI (critical assessment of predicted interactions) blind prediction experiment show that docking algorithms efficiently and accurately predict the mode of assembly of proteins that do not change conformation when they associate. They perform less well in the presence of large conformation changes and the experiment stimulates the development of novel procedures that can handle such changes.
机译：蛋白质晶体结构存入数据银行说明生物的多样性大分子识别:瞬态在蛋白质相互作用和蛋白质的DNA复合物和永久homodimeric总成蛋白质。大分子接口的属性可以控制的稳定性和特异性吗探索配合物和认可为与crystal-packing相比交互。接口通常要小得多;少比在原子和不太紧密特定的组件。埋葬1200 - 2000埃(2)蛋白质的表面发生在蛋白酶抑制剂和抗原抗体复合物的组装与很少或没有构象变化。电子转换复合物有小接口;观察复合物参与信号转导并为与经常存在的构象变化,与生物功能。卡普瑞(关键的评估预测交互)盲目预测实验表明对接算法有效准确预测的装配方式蛋白质时,不改变构象他们联系起来。构象变化和存在实验刺激的小说的发展程序可以处理这种变化。

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