Chapter title |
Structural Studies of ERK2 Protein Complexes.
|
---|---|
Chapter number | 4 |
Book title |
ERK Signaling
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6424-6_4 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6422-2, 978-1-4939-6424-6
|
Authors |
Johannes F. Weijman, Stefan J. Riedl, Peter D. Mace |
Editors |
Gerardo Jimenez |
Abstract |
ERK1 and ERK2 (ERK1/2) are the primary effector kinases of the RAS-RAF-MEK-ERK signaling pathway. A variety of substrates and regulatory partners associate with ERK1/2 through distinct D-peptide- and DEF-docking sites on their kinase domains. While understanding of D-peptides that bind to ERK1/2 has become increasingly clear over the last decade, only more recently have structures of proteins interacting with other binding sites on ERK1/2 become available. PEA-15 is a 130-residue ERK1/2 regulator that engages both the D-peptide- and DEF-docking sites of ERK kinases, and directly sequesters the ERK2 activation loop in various different phosphorylation states. Here we describe the methods used to derive crystallization-grade complexes of ERK2-PEA-15, which may also be adapted for other regulators that associate with the activation loop of ERK1/2. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 13 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 2 | 15% |
Researcher | 2 | 15% |
Student > Ph. D. Student | 1 | 8% |
Other | 1 | 8% |
Student > Master | 1 | 8% |
Other | 1 | 8% |
Unknown | 5 | 38% |
Readers by discipline | Count | As % |
---|---|---|
Chemistry | 3 | 23% |
Agricultural and Biological Sciences | 2 | 15% |
Biochemistry, Genetics and Molecular Biology | 2 | 15% |
Unknown | 6 | 46% |