Titlebook: Viral Membrane Proteins: Structure, Function, and Drug Design; Wolfgang B. Fischer Book 2005 Springer-Verlag US 2005 HIV.biochemistry.enzy

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Structure and Function of a Viral Encoded K+ Channel

Kinetic

Computer Simulations of Proton Transport Through the M2 Channel of the Influenza A Virus

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Virus Ion Channels Formed by Vpu of HIV-1, the 6K Protein of Alphaviruses and NB of Influenza B Viru

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Viral Membrane Proteins: Structure, Function, and Drug Design978-0-387-28146-9

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Influenza A Virus M2 Protein: Proton Selectivity of the Ion Channel, Cytotoxicity, and a Hypothesis rical or filamentous. The M2 protein has recently been shown to bind cholesterol, but cholesterol appeared nonessential for ion channel activity. The M2 endodomain contains a cholesterol-binding motif, which also occurs in HIV gp41. We propose that M2 is targeted to the raft periphery enabling it to

assent

Structure, Phosphorylation, and Biological Function of the HIV-1 Specific Virus Protein U (Vpu)Fas mediated apoptosis. Second, Vpu augments virus release from a post ER compartment by a cation-selective ion channel activity mediated by its transmembrane (TM) anchor. The phosphorylation of the molecule is mediated by the ubiquitous protein kinase caseinkinase 2 (CK-2) within a central conserve

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Solid-State NMR Investigations of Vpu Structural Domains in Oriented Phospholipid Bilayers: Interactt of structural domains of Vpu within the lipid membrane. Whereas the hydrophobic helix 1, which is located at the N-terminus, adopts a transmembrane tilt angle of approximately 20°, the amphipathic helix 2 in the center of the polypeptide is oriented parallel to the membrane surface. No major chang