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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Gilquin, Bernard Racapé, Judith Wrisch, Anja Visan, Violeta Lecoq, Alain Grissmer, Stephan Ménez, André Gasparini, Sylvaine |
| Abstract | A structural model of BgK, a sea anemone toxin, complexed with the S5-S6 region of Kv1.1, a voltage-gated potassium channel, was determined by flexible docking under distance restraints identified by a double mutant cycles approach. This structure provides the molecular basis for identifying the major determinants of the BgK-Kv1.1 channel interactions involving the BgK dyad residues Lys25 and Tyr26. These interactions are (i) electrostatic interactions between the extremity of Lys25 side chain and carbonyl oxygen atoms of residues from the channel selectivity filter that may be strengthened by solvent exclusion provided by (ii) hydrophobic interactions involving BgK residues Tyr26 and Phe6 and Kv1.1 residue Tyr379 whose side chain protrudes in the channel vestibule. In other Kv1 channel-BgK complexes, these interactions are likely to be conserved, implicating both conserved and variable residues from the channels. The data suggest that the conservation in sea anemone and scorpion potassium channel blockers of a functional dyad composed of a lysine, and a hydrophobic residue reflects their use of convergent binding solutions based on a crucial interplay between these important conserved interactions. |
| Related Links | http://www.jbc.org/content/277/40/37406.abstract |
| Ending Page | 37413 |
| Starting Page | 37406 |
| Page Count | 8 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 40 |
| Volume Number | 277 |
| DOI | 10.1074/jbc.M206205200 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2002-10-04 |
| Access Restriction | Open |
| Subject Keyword | Dendrotoxin (DTX) Human embryonic kidney (HEK) Rat basophilic leukemia (RBL) Root mean square deviation (r.m.s.d.) Wild type (wt) Mutant (mut) PROTEIN STRUCTURE AND FOLDING |
| Alternative Title | Structure of the BgK-Kv1.1 Complex Based on Distance Restraints Identified by Double Mutant Cycles |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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