NDLI: The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Please wait, while we are loading the content...

HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion

Effect of acyl chain structure and bilayer phase state on binding and penetration of a supported lipid bilayer by HPA3

Cyclic antimicrobial R-, W-rich peptides: the role of peptide structure and E. coli outer and inner membranes in activity and the mode of action

Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations

The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action

Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin

European Biophysics Journal : Volume 40, Issue 3, March 2011

European Biophysics Journal : Volume 40, Issue 2, February 2011

European Biophysics Journal : Volume 40, Issue 1, January 2011

European Biophysics Journal : Volume 39

European Biophysics Journal : Volume 38

European Biophysics Journal : Volume 37

European Biophysics Journal : Volume 36

European Biophysics Journal : Volume 35

European Biophysics Journal : Volume 34

European Biophysics Journal : Volume 33

European Biophysics Journal : Volume 32

European Biophysics Journal : Volume 31

European Biophysics Journal : Volume 30

European Biophysics Journal : Volume 29

European Biophysics Journal : Volume 28

European Biophysics Journal : Volume 27

European Biophysics Journal : Volume 26

European Biophysics Journal : Volume 25

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Content Provider	Springer Nature Link
Author	Theisgen, Stephan Thomas, Lars Schröder, Thomas Lange, Christian Kovermann, Michael Balbach, Jochen Huster, Daniel
Copyright Year	2011
Abstract	Guanylate cyclase-activating proteins (GCAPs) are neuronal Ca2+ sensors that play a central role in shaping the photoreceptor light response and in light adaptation through the Ca2+-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.
Starting Page	565
Ending Page	576
Page Count	12
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	40
Issue Number	4
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-02-17
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Lipid modification GCAP-2 Membrane-protein interaction Order parameter Biochemistry Cell Biology Nanotechnology Membrane Biology Neurobiology Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Guanylate Cyclase-Activating Protein-2 Undergoes Structural Changes upon Binding to Detergent Micelles and Bicelles

Dimerization Domain of Retinal Membrane Guanylyl Cyclase 1 (RetGC1) Is an Essential Part of Guanylyl Cyclase-activating Protein (GCAP) Binding Interface

Mapping Functional Domains of the Guanylate Cyclase Regulator Protein, GCAP-2

Molecular Details of Retinal Guanylyl Cyclase 1/GCAP-2 Interaction

Lipid model membranes for drug interaction study

Photoreceptor Guanylate Cyclase (GUCY2D) Mutations Cause Retinal Dystrophies by Severe Malfunction of Ca2+-Dependent Cyclic GMP Synthesis

Interaction between K+ channel gate modifier hanatoxin and lipid bilayer membranes analyzed by molecular dynamics simulation

Bicarbonate and Ca2+ Sensing Modulators Activate Photoreceptor ROS-GC1 Synergistically

A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Similar Documents

Guanylate Cyclase-Activating Protein-2 Undergoes Structural Changes upon Binding to Detergent Micelles and Bicelles

Dimerization Domain of Retinal Membrane Guanylyl Cyclase 1 (RetGC1) Is an Essential Part of Guanylyl Cyclase-activating Protein (GCAP) Binding Interface

Mapping Functional Domains of the Guanylate Cyclase Regulator Protein, GCAP-2

Molecular Details of Retinal Guanylyl Cyclase 1/GCAP-2 Interaction

Lipid model membranes for drug interaction study

Photoreceptor Guanylate Cyclase (GUCY2D) Mutations Cause Retinal Dystrophies by Severe Malfunction of Ca2+-Dependent Cyclic GMP Synthesis

Interaction between K+ channel gate modifier hanatoxin and lipid bilayer membranes analyzed by molecular dynamics simulation

Bicarbonate and Ca2+ Sensing Modulators Activate Photoreceptor ROS-GC1 Synergistically

A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2