KcsA closed and open: modelling and simulation studies.

Conference item

Bacterial homologues of mammalian potassium channels provide structures of two states of a gated K channel. Thus, the crystal structure of KcsA represents a closed state whilst that of MthK represents an open state. Using homology modelling and molecular dynamics simulations we have built a model of the transmembrane domain of KcsA in an open state and have compared its conformational stability with that of the same domain of KcsA in a closed state. Approximate Born energy calculations of mon...

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Authors: Holyoake, J; Domene, C; Bright, J; Sansom, MS

• Publication status: Published
• Host title: European biophysics journal : EBJ
• Volume: 33
• Issue: 3
• Pages: 238-246
• Publication date: 2004-05-01
• Event location: Germany
• DOI: 10.1007/s00249-003-0355-2
• EISSN: 1432-1017
• ISSN: 0175-7571
• Keywords: Permeability; Protein Structure, Secondary; Potassium Channels; Bacterial Proteins; Animals; Hydrophobic and Hydrophilic Interactions; Receptors, Nicotinic; Ribosomal Proteins; Humans; Prokaryotic Cells; Crystallography, X-Ray; Computer Simulation; Protein Conformation; Models, Molecular