Data set for "Structural diversity in <i>de novo</i> cyclic peptide ligands from genetically encoded library technologies"

The related publication reviews the cyclic peptides identified through these techniques reported in the period 2015 to 2019, with a particular focus on the three-dimensional structures that peptides adopt when binding to their targets. It also highlights examples where co-crystal structures have informed the key interactions that promote high affinity and selectivity of cyclic peptides against their targets, identified novel inhibitor binding sites, and provided new insights into the biology of their targets.This dataset comprises contents of tables 1 and 2 with additional data as used in figures 1 and 2.Table 1: Overview of recent CPs identified through genetically encoded library techniques against protein targets.Table 2: X-ray crystal structures of CPs in complex with their targets.The figures referenced are briefly described below:Figure 1: Calculated physicochemical properties of cyclic peptides identified through selection technologies.Figure 2: Properties of cyclic peptides co-crystallised with their target.本相关综述梳理了2015至2019年间通过各类技术所鉴定得到的环肽（cyclic peptides），并特别聚焦于环肽与靶点结合时所呈现的三维构象。该综述同时列举了诸多典型案例：共晶结构（co-crystal structures）阐明了介导环肽与靶点产生高亲和力与选择性的关键相互作用，明确了新型抑制剂结合位点，并为解析靶点的生物学机制提供了全新视角。本数据集包含表1、表2的全部内容，以及图1与图2中所用到的补充数据。表1：通过基因编码文库技术鉴定得到的靶向蛋白靶点的近期环肽（cyclic peptides，简称CPs）概览。表2：环肽与靶点形成复合物的X射线晶体结构（X-ray crystal structures）。下文将对所引用的图表进行简要说明：图1：通过筛选技术鉴定得到的环肽的计算理化性质（physicochemical properties）。图2：与靶点共结晶的环肽的相关特性。