Chapter title |
Crystallization of Mouse RIG-I ATPase Domain: In Situ Proteolysis.
|
---|---|
Chapter number | 3 |
Book title |
Innate DNA and RNA Recognition
|
Published in |
Methods in molecular biology, May 2014
|
DOI | 10.1007/978-1-4939-0882-0_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-0881-3, 978-1-4939-0882-0
|
Authors |
Civril F, Hopfner KP, Filiz Civril, Karl-Peter Hopfner |
Editors |
Hans-Joachim Anders, Adriana Migliorini |
Abstract |
RIG-I is a key pattern recognition receptor that recognizes cytoplasmic viral RNA. Upon ligand binding, it undergoes a conformational change that induces an active signaling conformation. However, the details of this conformational change remain elusive until high-resolution crystal structures of different functional conformations are available. X-ray crystallography is a powerful tool to study structure-function relationships, but crystallization is often the limiting step of the method. Here, we describe the in situ in-drop proteolysis of RIG-I that yielded crystals of the ATPase domain of mouse RIG-I suitable for structure determination. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 3 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Professor | 1 | 33% |
Student > Bachelor | 1 | 33% |
Researcher | 1 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 2 | 67% |
Chemistry | 1 | 33% |