PDF(Pubmed)
Abstract：
Mutations in the FKBP14 gene encoding the endoplasmic reticulum resident collagen-related proline isomerase FK506 binding protein 22 kDa (FKBP22) result in kyphoscoliotic Ehlers-Danlos Syndrome (EDS), which is characterized by a broad phenotypic outcome. A plausible explanation for this outcome is that FKBP22 participates in the biosynthesis of subsets of collagen types: FKBP22 selectively binds to collagens III, IV, VI, and X, but not to collagens I, II, V, and XI. However, these binding mechanisms have never been explored, and they may underpin EDS subtype heterogeneity. Here, we used collagen Toolkit peptide libraries to investigate binding specificity. We observed that FKBP22 binding was distributed along the collagen helix. Further, it (1) was higher on collagen III than collagen II peptides and it (2) was correlated with a positive peptide charge. These findings begin to elucidate the mechanism by which FKBP22 interacts with collagen.
摘要：
编码内质网驻留胶原相关脯氨酸异构酶FK506结合蛋白22kDa（FKBP22）的FKBP14基因的突变导致后凸脊柱侧耳Ehlers-Danlos综合征（EDS），其特征是广泛的表型结果。对这一结果的一个合理的解释是FKBP22参与胶原蛋白类型亚群的生物合成：FKBP22选择性地结合胶原蛋白III，IV,VI,X,但不是我的胶原蛋白，II,V,和XI。然而,这些约束机制从未被探索过，它们可能支持EDS亚型异质性。这里,我们使用胶原蛋白Toolkit肽文库来研究结合特异性.我们观察到FKBP22结合沿着胶原螺旋分布。Further,它（1）在胶原蛋白III上比胶原蛋白II肽高，并且它（2）与正肽电荷相关。这些发现开始阐明FKBP22与胶原蛋白相互作用的机制。
