Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide
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چکیده
منابع مشابه
Anionic phospholipids are determinants of membrane protein topology.
The orientation of many membrane proteins is determined by the asymmetric distribution of positively charged amino acid residues in cytoplasmic and translocated loops. The positive-inside rule states that loops with large amounts of these residues tend to have cytoplasmic locations. Orientations of constructs derived from the inner membrane protein leader peptidase from Escherichia coli were fo...
متن کاملModeling peptide binding to anionic membrane pores
Peptide-induced pore formation in membranes can be dissected into two steps: pore formation and peptide binding to the pore. A computational method is proposed to study the second step in anionic membranes. The electrostatic potential is obtained from numerical solutions to the Poisson-Boltzmann equation and is then used in conjunction with IMM1 (implicit membrane model 1). A double charge laye...
متن کاملBound anionic states of adenine.
Anionic states of nucleic acid bases are involved in DNA damage by low-energy electrons and in charge transfer through DNA. Previous gas phase studies of free, unsolvated nucleic acid base parent anions probed only dipole-bound states, which are not present in condensed phase environments, but did not observe valence anionic states, which for purine bases are thought to be adiabatically unbound...
متن کاملCharacterisation of a Binding Site for Anionic Phospholipids on Kcnq1
CHARACTERISATION OF A BINDING SITE FOR ANIONIC PHOSPHOLIPIDS ON KCNQ1 Alison M. Thomas, Stephen C. Harmer, Tapsi Khambra & Andrew Tinker From the Department of Medicine, University College London, 5 University Street, London, WC1E 6JJ, UK. Running Title: A PIP2 binding site on KCNQ1 * These authors contributed equally to this study Address correspondence to: Professor Andrew Tinker, Department ...
متن کاملCharacterization of a binding site for anionic phospholipids on KCNQ1.
The KCNQ family of potassium channels underlie a repolarizing K(+) current in the heart and the M-current in neurones. The assembly of KCNQ1 with KCNE1 generates the delayed rectifier current I(Ks) in the heart. Characteristically these channels are regulated via G(q/11)-coupled receptors and the inhibition seen after phospholipase C activation is now thought to occur from membrane phosphatidyl...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1995
ISSN: 0014-5793
DOI: 10.1016/0014-5793(95)00823-r