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The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2
by
Balbach, Jochen
, Thomas, Lars
, Lange, Christian
, Schröder, Thomas
, Theisgen, Stephan
, Kovermann, Michael
, Huster, Daniel
in
Amino acids
/ Binding
/ Biochemistry
/ Biological and Medical Physics
/ Biomedical and Life Sciences
/ Biophysics
/ Calcium
/ Calcium ions
/ Calcium-Binding Proteins - chemistry
/ Calcium-Binding Proteins - metabolism
/ Cell Biology
/ Cellular biology
/ Crystal structure
/ Detergents
/ Glucose
/ Guanylate cyclase
/ Guanylate Cyclase-Activating Proteins - analysis
/ Guanylate Cyclase-Activating Proteins - chemistry
/ Guanylate Cyclase-Activating Proteins - metabolism
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Life Sciences
/ Light adaptation
/ Lipid bilayers
/ Lipid Bilayers - chemistry
/ Lipid Bilayers - pharmacology
/ Lipid membranes
/ Lipids
/ Liposomes - chemistry
/ Liposomes - pharmacology
/ Magnetic Resonance Spectroscopy - methods
/ Membrane Biology
/ Membranes
/ Micelles
/ Myristic Acid - chemistry
/ Myristic Acid - pharmacology
/ N-Terminus
/ Nanotechnology
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neurobiology
/ Neurons
/ NMR
/ Nuclear magnetic resonance
/ Original Paper
/ Phosphatidylcholines - chemistry
/ Phosphatidylcholines - pharmacology
/ Photoreceptor Cells - drug effects
/ Photoreceptor Cells - metabolism
/ Protein Binding
/ Protein structure
/ Proteins
/ Retina - drug effects
/ Retina - metabolism
/ Temperature
2011
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The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2
by
Balbach, Jochen
, Thomas, Lars
, Lange, Christian
, Schröder, Thomas
, Theisgen, Stephan
, Kovermann, Michael
, Huster, Daniel
in
Amino acids
/ Binding
/ Biochemistry
/ Biological and Medical Physics
/ Biomedical and Life Sciences
/ Biophysics
/ Calcium
/ Calcium ions
/ Calcium-Binding Proteins - chemistry
/ Calcium-Binding Proteins - metabolism
/ Cell Biology
/ Cellular biology
/ Crystal structure
/ Detergents
/ Glucose
/ Guanylate cyclase
/ Guanylate Cyclase-Activating Proteins - analysis
/ Guanylate Cyclase-Activating Proteins - chemistry
/ Guanylate Cyclase-Activating Proteins - metabolism
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Life Sciences
/ Light adaptation
/ Lipid bilayers
/ Lipid Bilayers - chemistry
/ Lipid Bilayers - pharmacology
/ Lipid membranes
/ Lipids
/ Liposomes - chemistry
/ Liposomes - pharmacology
/ Magnetic Resonance Spectroscopy - methods
/ Membrane Biology
/ Membranes
/ Micelles
/ Myristic Acid - chemistry
/ Myristic Acid - pharmacology
/ N-Terminus
/ Nanotechnology
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neurobiology
/ Neurons
/ NMR
/ Nuclear magnetic resonance
/ Original Paper
/ Phosphatidylcholines - chemistry
/ Phosphatidylcholines - pharmacology
/ Photoreceptor Cells - drug effects
/ Photoreceptor Cells - metabolism
/ Protein Binding
/ Protein structure
/ Proteins
/ Retina - drug effects
/ Retina - metabolism
/ Temperature
2011
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The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2
by
Balbach, Jochen
, Thomas, Lars
, Lange, Christian
, Schröder, Thomas
, Theisgen, Stephan
, Kovermann, Michael
, Huster, Daniel
in
Amino acids
/ Binding
/ Biochemistry
/ Biological and Medical Physics
/ Biomedical and Life Sciences
/ Biophysics
/ Calcium
/ Calcium ions
/ Calcium-Binding Proteins - chemistry
/ Calcium-Binding Proteins - metabolism
/ Cell Biology
/ Cellular biology
/ Crystal structure
/ Detergents
/ Glucose
/ Guanylate cyclase
/ Guanylate Cyclase-Activating Proteins - analysis
/ Guanylate Cyclase-Activating Proteins - chemistry
/ Guanylate Cyclase-Activating Proteins - metabolism
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Life Sciences
/ Light adaptation
/ Lipid bilayers
/ Lipid Bilayers - chemistry
/ Lipid Bilayers - pharmacology
/ Lipid membranes
/ Lipids
/ Liposomes - chemistry
/ Liposomes - pharmacology
/ Magnetic Resonance Spectroscopy - methods
/ Membrane Biology
/ Membranes
/ Micelles
/ Myristic Acid - chemistry
/ Myristic Acid - pharmacology
/ N-Terminus
/ Nanotechnology
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neurobiology
/ Neurons
/ NMR
/ Nuclear magnetic resonance
/ Original Paper
/ Phosphatidylcholines - chemistry
/ Phosphatidylcholines - pharmacology
/ Photoreceptor Cells - drug effects
/ Photoreceptor Cells - metabolism
/ Protein Binding
/ Protein structure
/ Proteins
/ Retina - drug effects
/ Retina - metabolism
/ Temperature
2011
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The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2
Journal Article
The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2
2011
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Overview
Guanylate cyclase-activating proteins (GCAPs) are neuronal Ca
2+
sensors that play a central role in shaping the photoreceptor light response and in light adaptation through the Ca
2+
-dependent regulation of the transmembrane retinal guanylate cyclase. GCAPs are N-terminally myristoylated, and the role of the myristoyl moiety is not yet fully understood. While protein lipid chains typically represent membrane anchors, the crystal structure of GCAP-1 showed that the myristoyl chain of the protein is completely buried within a hydrophobic pocket of the protein, which stabilizes the protein structure. Therefore, we address the question of the localization of the myristoyl group of GCAP-2 in the absence and in the presence of lipid membranes as well as DPC detergents (as a membrane substitute amenable to solution state NMR). We investigate membrane binding of both myristoylated and nonmyristoylated GCAP-2 and study the structure and dynamics of the myristoyl moiety of GCAP-2 in the presence of POPC membranes. Further, we address structural alterations within the myristoylated N-terminus of GCAP-2 in the presence of membrane mimetics. Our results suggest that upon membrane binding the myristoyl group is released from the protein interior and inserts into the lipid bilayer.
Publisher
Springer-Verlag,Springer Nature B.V
Subject
/ Binding
/ Biological and Medical Physics
/ Biomedical and Life Sciences
/ Calcium
/ Calcium-Binding Proteins - chemistry
/ Calcium-Binding Proteins - metabolism
/ Glucose
/ Guanylate Cyclase-Activating Proteins - analysis
/ Guanylate Cyclase-Activating Proteins - chemistry
/ Guanylate Cyclase-Activating Proteins - metabolism
/ Hydrophobic and Hydrophilic Interactions
/ Lipid Bilayers - pharmacology
/ Lipids
/ Magnetic Resonance Spectroscopy - methods
/ Micelles
/ Myristic Acid - pharmacology
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neurons
/ NMR
/ Phosphatidylcholines - chemistry
/ Phosphatidylcholines - pharmacology
/ Photoreceptor Cells - drug effects
/ Photoreceptor Cells - metabolism
/ Proteins
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