| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10760888 | Biochemical and Biophysical Research Communications | 2012 | 6 Pages |
Abstract
⺠X-ray crystal and SAXS experiments represented a transient state of apo npMAP2K4. ⺠Formation of β-barrel conferred the ATP site to be exposed to the bulk solvent. ⺠This conformation displayed the transient state after the product ADP release. ⺠The ATP binding allows the transient structure to assume the canonical kinase fold. ⺠The depletion of ATP perhaps enhances the aggregation via hydrophobic interactions.
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Authors
Takashi Matsumoto, Takayoshi Kinoshita, Yasuyuki Kirii, Toshiji Tada, Akihito Yamano,