Advances in chaperone-assisted RNA crystallography using synthetic antibodies

Thumbnail Image

Files

1-s2.0-S2667160323000303-main.pdf (6.72 MB)

Links to Files

https://www.sciencedirect.com/science/article/pii/S2667160323000303

Permanent Link

https://doi.org/10.1016/j.bbadva.2023.100101
 http://hdl.handle.net/11603/29534

Collections

UMBC Chemistry & Biochemistry Department
UMBC Faculty Collection
UMBC Student Collection

Author/Creator

Author/Creator ORCID

https://orcid.org/0000-0001-7475-6706
 https://orcid.org/0000-0002-5308-2746
 https://orcid.org/0009-0001-3907-431X
 https://orcid.org/0000-0001-6424-3173

Date

2023-08-21

Type of Work

journal articles
Text

Department

Program

Citation of Original Publication

Banna, Hasan Al, Naba Krishna Das, Manju Ojha, and Deepak Koirala. “Advances in Chaperone-Assisted RNA Crystallography Using Synthetic Antibodies.” BBA Advances 4 (January 1, 2023): 100101. https://doi.org/10.1016/j.bbadva.2023.100101.

Rights

This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)

Subjects

Abstract

RNA molecules play essential roles in many biological functions, from gene expression regulation, cellular growth, and metabolism to catalysis. They frequently fold into three-dimensional structures to perform their functions. Therefore, determining RNA structure represents a key step for understanding the structure-function relationships and developing RNA-targeted therapeutics. X-ray crystallography remains a method of choice for determining high-resolution RNA structures, but it has been challenging due to difficulties associated with RNA crystallization and phasing. Several natural and synthetic RNA binding proteins have been used to facilitate RNA crystallography. Having unique properties to help crystal packing and phasing, synthetic antibody fragments, specifically the Fabs, have emerged as promising RNA crystallization chaperones, and so far, over a dozen of RNA structures have been solved using this strategy. Nevertheless, multiple steps in this approach need to be improved, including the recombinant expression of these anti-RNA Fabs, to warrant the full potential of these synthetic Fabs as RNA crystallization chaperones. This review highlights the nuts and bolts and recent advances in the chaperone-assisted RNA crystallography approach, specifically emphasizing the Fab antibody fragments as RNA crystallization chaperones.