Structure-Dynamic Coupling Through Ca2+-Binding Regulatory Domains of Mammalian NCX Isoform/Splice Variants

2017 ◽  
pp. 41-58 ◽  
Author(s):  
Daniel Khananshvili
Keyword(s):  
Splice Variants ◽  
Dynamic Coupling ◽  
Regulatory Domains ◽  
Structure Dynamic

Structure-dynamic determinants governing a mode of regulatory response and propagation of allosteric signal in splice variants of Na+/Ca2+ exchange (NCX) proteins

2015 ◽  
Vol 465 (3) ◽  
pp. 489-501 ◽  
Author(s):  
Moshe Giladi ◽  
Su Youn Lee ◽  
Reuben Hiller ◽  
Ka Young Chung ◽  
Daniel Khananshvili
Keyword(s):  
Calcium Binding ◽  
Splice Variant ◽  
Main Chain ◽  
Splice Variants ◽  
Binding Domain ◽  
Dependent Manner ◽  
Regulatory Response ◽  
Structure Dynamic ◽  
Calcium Binding Domain

Ca2+ binding to CBD1 (calcium-binding domain 1) and CBD2 regulates Na+/Ca2+ exchangers (NCX). In the present study, we demonstrate that Ca2+ binding rigidifies the main chain of CBD2, but not of CBD1, in a splice variant-dependent manner. The dynamic differences account for variant-dependent responses to Ca2+.

scholarly journals Identification of a haem domain in human soluble adenylate cyclase

2012 ◽  
Vol 32 (5) ◽  
pp. 491-499 ◽  
Author(s):  
Sabine Middelhaufe ◽  
Martina Leipelt ◽  
Lonny R. Levin ◽  
Jochen Buck ◽  
Clemens Steegborn
Keyword(s):  
Skeletal Muscle ◽  
Splice Variants ◽  
Second Messengers ◽  
Class Iii ◽  
Catalytic Core ◽  
Unique Type ◽  
Transmembrane Receptors ◽  
Regulatory Domains ◽  
Physiological Processes ◽  
Axial Ligands

The second messengers cAMP and cGMP mediate a multitude of physiological processes. In mammals, these cyclic nucleotides are formed by related Class III nucleotidyl cyclases, and both ACs (adenylate cyclases) and GCs (guanylate cyclases) comprise transmembrane receptors as well as soluble isoforms. Whereas sGC (soluble GC) has a well-characterized regulatory HD (haem domain) that acts as a receptor for the activator NO (nitric oxide), very little is known about the regulatory domains of the ubiquitous signalling enzyme sAC (soluble AC). In the present study, we identify a unique type of HD as a regulatory domain in sAC. The sAC-HD (sAC haem domain) forms a larger oligomer and binds, non-covalently, one haem cofactor per monomer. Spectral analyses and mutagenesis reveal a 6-fold co-ordinated haem iron atom, probably with non-typical axial ligands, which can bind both NO and CO (carbon monoxide). Splice variants of sAC comprising this domain are expressed in testis and skeletal muscle, and the HD displays an activating effect on the sAC catalytic core. Our results reveal a novel mechanism for regulation of cAMP signalling and suggest a need for reanalysis of previous studies on mechanisms of haem ligand effects on cyclic nucleotide signalling, particularly in testis and skeletal muscle.

Expression of splice variants; The human cholecystokinin-B receptor in association with gastrointestinal cancer

2001 ◽  
Vol 120 (5) ◽  
pp. A507-A507
Author(s):  
D KANG ◽  
Y WHANG ◽  
J YOO ◽  
I SONG ◽  
J OH ◽  
...  
Keyword(s):  
Gastrointestinal Cancer ◽  
Splice Variants

Fast structure-dynamic simulation of electrical machines using 2d-3d coupling

2007 ◽  
Vol 2 (1) ◽  
pp. 3-15 ◽  
Author(s):  
Christoph Schlensok ◽  
Kay Hameyer
Keyword(s):  
Dynamic Simulation ◽  
Electrical Machines ◽  
Structure Dynamic
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