scholarly journals Crystal Structure of the Ligand Binding Suppressor Domain of Type 1 Inositol 1,4,5-Trisphosphate Receptor

2005 ◽  
Vol 17 (2) ◽  
pp. 193-203 ◽  
Author(s):  
Ivan Bosanac ◽  
Haruka Yamazaki ◽  
Toru Matsu-ura ◽  
Takayuki Michikawa ◽  
Katsuhiko Mikoshiba ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals Ca2+ and calmodulin differentially modulate myo-inositol 1,4,5-trisphosphate (IP3)-binding to the recombinant ligand-binding domains of the various IP3 receptor isoforms

2000 ◽  
Vol 346 (2) ◽  
pp. 275-280 ◽  
Author(s):  
Sara VANLINGEN ◽  
Henk SIPMA ◽  
Patrick DE SMET ◽  
Geert CALLEWAERT ◽  
Ludwig MISSIAEN ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Recombinant Proteins ◽  
Ip3 Receptor ◽  
Binding Characteristics ◽  
Binding Domains ◽  
Receptor Isoforms ◽  
Inositol 1,4,5 Trisphosphate ◽  
Adenophostin A ◽  
Trisphosphate Receptor

We have expressed the N-terminal 581 amino acids of type 1 myo-inositol 1,4,5-trisphosphate receptor (IP3R1), IP3R2 and IP3R3 as recombinant proteins [ligand-binding site 1 (lbs-1), lbs-2, lbs-3] in the soluble fraction of Escherichia coli. These recombinant proteins contain the complete IP3-binding domain and bound IP3 and adenophostin A with high affinity. Ca2+ and calmodulin were previously found to maximally inhibit IP3 binding to lbs-1 by 42±6 and 43±6% respectively, and with an IC50 of approx. 200 nM and 3 μM respectively [Sipma, De Smet, Sienaert, Vanlingen, Missiaen, Parys and De Smedt (1999) J. Biol. Chem. 274, 12157-12562]. We now report that Ca2+ inhibited IP3 binding to lbs-3 with an IC50 of approx. 700 nM (37±4% inhibition at 5 μM Ca2+), while IP3 binding to lbs-2 was not affected by increasing [Ca2+] from 100 nM to 25 μM. Calmodulin (10 μM) inhibited IP3 binding to lbs-3 by 37±4%, while IP3 binding to lbs-2 was inhibited by only 11±2%. The inhibition of IP3 binding to lbs-3 by calmodulin was dose-dependent (IC50≈ 2 μM). We conclude that the IP3-binding domains of the various IP3R isoforms differ in binding characteristics for IP3 and adenophostin A, and are differentially modulated by Ca2+ and calmodulin, suggesting that the various IP3R isoforms can have different intracellular functions.

scholarly journals Tyr-167/Trp-168 in Type 1/3 Inositol 1,4,5-Trisphosphate Receptor Mediates Functional Coupling between Ligand Binding and Channel Opening

2010 ◽  
Vol 285 (46) ◽  
pp. 36081-36091 ◽  
Author(s):  
Haruka Yamazaki ◽  
Jenny Chan ◽  
Mitsuhiko Ikura ◽  
Takayuki Michikawa ◽  
Katsuhiko Mikoshiba
Keyword(s):  
Ligand Binding ◽  
Functional Coupling ◽  
Channel Opening ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

Differential modulation of inositol 1,4,5-trisphosphate receptor type 1 and type 3 by ATP

Cell Calcium ◽  
2000 ◽  
Vol 27 (5) ◽  
pp. 257-267 ◽  
Author(s):  
K. Maes ◽  
L. Missiaen ◽  
P. De Smet ◽  
S. Vanlingen ◽  
G. Callewaert ◽  
...  
Keyword(s):  
Receptor Type ◽  
Differential Modulation ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3

scholarly journals The Type 1 Inositol 1,4,5-Trisphosphate Receptor Gene Is Altered in theopisthotonosMouse

1997 ◽  
Vol 17 (2) ◽  
pp. 635-645 ◽  
Author(s):  
Valerie A. Street ◽  
Martha M. Bosma ◽  
Vasiliki P. Demas ◽  
Melissa R. Regan ◽  
Doras D. Lin ◽  
...  
Keyword(s):  
Receptor Gene ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

Differential Levels and Phosphorylation of Type 1 Inositol 1,4,5-Trisphosphate Receptor in Four Different Murine Models of Huntington Disease

2019 ◽  
Vol 8 (3) ◽  
pp. 271-289
Author(s):  
Joakim Iver Post ◽  
Trygve B. Leergaard ◽  
Veronika Ratz ◽  
S. Ivar Walaas ◽  
Stephan von Hörsten ◽  
...  
Keyword(s):  
Huntington Disease ◽  
Murine Models ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor
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