Analysis of Fbox substrate adapter proteins using ProteoSync, a program for projection of evolutionary conservation onto protein atomic coordinates

The projection of conservation onto the surface of a protein’s 3D structure is a powerful way of inferring functionally important regions. For this reason, we created ProteoSync, a Python program that semi-automates the process. The program creates an annotated sequence alignment of orthologs from a...

وصف كامل

التفاصيل البيبلوغرافية
الحاوية / القاعدة:Computational and Structural Biotechnology Journal
المؤلفون الرئيسيون: Elliot Sicheri, Daniel Mao, Michael Tyers, Frank Sicheri
التنسيق: مقال
اللغة:الإنجليزية
منشور في: Elsevier 2025-01-01
الموضوعات:
الوصول للمادة أونلاين:http://www.sciencedirect.com/science/article/pii/S2001037025003721
الوصف
الملخص:The projection of conservation onto the surface of a protein’s 3D structure is a powerful way of inferring functionally important regions. For this reason, we created ProteoSync, a Python program that semi-automates the process. The program creates an annotated sequence alignment of orthologs from a diverse set of selectable species and enables the fast projection of amino acid conservation onto a predicted or known 3D model in PyMOL 1. As a test case, we used ProteoSync to analyze a subset of 31 F-box proteins, which function as substrate recognition subunits for a large family of Cul1-based E3 ubiquitin ligases. We correctly identified known substrate interaction surfaces for 11 F-box members with previously solved structures. We also identified likely ligand binding sites for 16 other members, thus demonstrating ProteoSync’s utility for discovering conserved, functionally relevant surfaces.
تدمد:2001-0370