Retinal guanylate cyclases (RetGCs) are regulated by a family of guanylate cyclase-activating proteins (called GCAP1-7). GCAPs form dimers that bind to Ca^(2+) and confer Ca^(2+) sensitive activation of RetGC during visual phototransduction. The GCAP5 homologue from zebrafish contains two nonconserved cysteine residues (Cys15 and Cys17) that bind to ferrous ion, which stabilizes GCAP5 dimerization and diminishes its ability to activate RetGC. Here, we present NMR and EPR-DEER structural analysis...
[ASAP] NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors
NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00612/20211005/images/medium/bi1c00612_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00612
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Structural Characterization of Ferrous Ion Bindingto Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors
Structural Characterization of Ferrous Ion Bindingto Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01029/20171206/images/medium/bi-2017-010292_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01029
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12-08-2017 01:06 AM
[NMR paper] Efficient long-distance NMR-PRE and EPR-DEER restraints for two-domain protein structure determination.
Efficient long-distance NMR-PRE and EPR-DEER restraints for two-domain protein structure determination.
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Protein Cell. 2013 Nov 27;
Authors: Wu K, Shi C, Li J, Wang H, Shi P, Chen L, Wu F, Xiong Y, Tian C
PMID: 24282082
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11-28-2013 05:18 PM
DEER-Stitch: Combining three- and four-pulse DEER measurements for high sensitivity, deadtime free data
DEER-Stitch: Combining three- and four-pulse DEER measurements for high sensitivity, deadtime free data
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
J.E. Lovett, B.W. Lovett, J. Harmer</br>
Over approximately the last fifteen years the electron paramagnetic resonance (EPR) technique of double electron electron resonance (DEER) has attracted considerable attention since it allows for the precise measurement of the dipole-dipole coupling between radicals and thus can lead to distance information between pairs of radicals separated by up to ca. 8 nm....
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08-22-2012 02:13 AM
[NMR paper] The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate s
The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Related Articles The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30
Authors: Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kühne R, Bermel W, Bacher A, Richter G, Oschkinat H
Recent developments in...
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11-19-2010 08:44 PM
[NMR paper] Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and
Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and NMR studies.
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Mol Genet Metab. 1998 Jan;63(1):14-25
Authors: Waring AJ, Chen Y, Faull KF, Stevens R, Sherman MA, Fluharty AL
Cerebroside sulfate activator protein (CSAct or saposin B) is one of a group of heat stable, low-molecular-weight proteins that appear to share a common structural motif. These have been referred to as saposin-like proteins...
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11-17-2010 11:06 PM
[NMR paper] NMR secondary structure of the plasminogen activator protein staphylokinase.
NMR secondary structure of the plasminogen activator protein staphylokinase.
Related Articles NMR secondary structure of the plasminogen activator protein staphylokinase.
J Biomol NMR. 1997 Apr;9(3):273-86
Authors: Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR
Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcus aureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolytic system, into plasmin, Sak is presently undergoing clinical trials for...
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08-22-2010 03:31 PM
[NMR paper] NMR secondary structure of the plasminogen activator protein staphylokinase.
NMR secondary structure of the plasminogen activator protein staphylokinase.
Related Articles NMR secondary structure of the plasminogen activator protein staphylokinase.
J Biomol NMR. 1997 Apr;9(3):273-86
Authors: Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR
Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcus aureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolytic system, into plasmin, Sak is presently undergoing clinical trials for...