Crystallization of a Complex Between MYC and Jas Motif.
Publication
, Chapter
Zhang, F; He, SY; Melcher, K
January 2020
In the jasmonate signaling pathway, a region of 17 amino acids within the Jas motif of JAZ proteins and a conserved region within the N-terminus of MYC proteins are sufficient for JAZ-MYC interactions. Crystal structures of Jas-MYC complexes have revealed the structural basis of this important interaction. Here, we describe methods of cloning, expression, and purification of MYC N-terminal proteins and their co-crystallization with Jas motif peptides.
Duke Scholars
DOI
Publication Date
January 2020
Volume
2085
Start / End Page
133 / 144
Related Subject Headings
- Repressor Proteins
- Recombinant Proteins
- Proto-Oncogene Proteins c-myc
- Multiprotein Complexes
- Gene Expression
- Developmental Biology
- Crystallization
- Cloning, Molecular
- Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
- Arabidopsis
Citation
APA
Chicago
ICMJE
MLA
NLM
Zhang, F., He, S. Y., & Melcher, K. (2020). Crystallization of a Complex Between MYC and Jas Motif. (Vol. 2085, pp. 133–144). https://doi.org/10.1007/978-1-0716-0142-6_10
Zhang, Feng, Sheng Yang He, and Karsten Melcher. “Crystallization of a Complex Between MYC and Jas Motif.,” 2085:133–44, 2020. https://doi.org/10.1007/978-1-0716-0142-6_10.
Zhang F, He SY, Melcher K. Crystallization of a Complex Between MYC and Jas Motif. In 2020. p. 133–44.
Zhang, Feng, et al. Crystallization of a Complex Between MYC and Jas Motif. Vol. 2085, 2020, pp. 133–44. Epmc, doi:10.1007/978-1-0716-0142-6_10.
Zhang F, He SY, Melcher K. Crystallization of a Complex Between MYC and Jas Motif. 2020. p. 133–144.
DOI
Publication Date
January 2020
Volume
2085
Start / End Page
133 / 144
Related Subject Headings
- Repressor Proteins
- Recombinant Proteins
- Proto-Oncogene Proteins c-myc
- Multiprotein Complexes
- Gene Expression
- Developmental Biology
- Crystallization
- Cloning, Molecular
- Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
- Arabidopsis