Draper D E, Reynaldo L P
Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.
Nucleic Acids Res. 1999 Jan 15;27(2):381-8. doi: 10.1093/nar/27.2.381.
Structures of a number of ribosomal proteins have now been determined by crystallography and NMR, though the complete structure of a ribosomal protein-rRNA complex has yet to be solved. However, some ribosomal protein structures show strong similarity to well-known families of DNA or RNA binding proteins for which structures in complex with cognate nucleic acids are available. Comparison of the known nucleic acid binding mechanisms of these non-ribosomal proteins with the most highly conserved surfaces of similar ribosomal proteins suggests ways in which the ribosomal proteins may be binding RNA. Three binding motifs, found in four ribosomal proteins so far, are considered here: homeodomain-like alpha-helical proteins (L11), OB fold proteins (S1 and S17) and RNP consensus proteins (S6). These comparisons suggest that ribosomal proteins combine a small number of fundamental strategies to develop highly specific RNA recognition sites.
目前，已有多种核糖体蛋白的结构通过晶体学和核磁共振得以确定，不过核糖体蛋白-rRNA复合物的完整结构尚未解析出来。然而，一些核糖体蛋白结构与已知的DNA或RNA结合蛋白家族具有很强的相似性，这些家族的蛋白与同源核酸形成复合物的结构是已知的。将这些非核糖体蛋白已知的核酸结合机制与相似核糖体蛋白的高度保守表面进行比较，有助于揭示核糖体蛋白与RNA的结合方式。本文探讨了迄今在四种核糖体蛋白中发现的三种结合基序：类同源结构域的α螺旋蛋白（L11）、OB折叠蛋白（S1和S17）以及RNP共有蛋白（S6）。这些比较表明，核糖体蛋白通过结合少数基本策略来形成高度特异性的RNA识别位点。
