IndraLab

Statements

KCNA3 binds mgt. 5 / 5
| 5
sparser
"Acetylation or biotinylation of the amino group reduced binding (10-fold) of MgTX to Kv1.3, suggesting the involvement of the N-terminal amino group in the toxin activity [30] ."
9395089
sparser
"As MgTx specifically binds to the pore of Kv1.3 with very high affinity (IC 50 : 110 pM), an excess of MgTx (5 μM) will prevent binding of Bax to Kv1.3, but only if Bax binds in the pore region of Kv1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
20114030
sparser
"The simulations suggest that MgTx-Lys35 occludes the ion conduction pathway of the channel on the formation of the MgTx-Kv1.3 complex, while Lys28 of the toxin stabilizes the complex by forming an additional salt bridge with Asp449, located just outside of the selectivity filter."
25054783
sparser
"We examine the binding of MgTx to Kv1.3 using molecular dynamics with distance restraint."
25054783
sparser
"We construct the potential of mean force (PMF) profile of the binding of the MgTx-Kv1.3 complex predicted from our simulations."
25054783