| Autor: |
Matthew C Clifton, David M Dranow, Alison Leed, Ben Fulroth, James W Fairman, Jan Abendroth, Kateri A Atkins, Ellen Wallace, Dazhong Fan, Guoping Xu, Z J Ni, Doug Daniels, John Van Drie, Guo Wei, Alex B Burgin, Todd R Golub, Brian K Hubbard, Michael H Serrano-Wu |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
PLoS ONE, Vol 10, Iss 4, p e0125010 (2015) |
| Druh dokumentu: |
article |
| ISSN: |
1932-6203 |
| DOI: |
10.1371/journal.pone.0125010 |
| Popis: |
Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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