This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3ox6
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3ox6.jpg|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3ox6", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3ox6| PDB=3ox6 | SCENE= }} | {{STRUCTURE_3ox6| PDB=3ox6 | SCENE= }} | ||
| - | |||
===Crystal Structure of the calcium sensor calcium-binding protein 1 (CaBP1)=== | ===Crystal Structure of the calcium sensor calcium-binding protein 1 (CaBP1)=== | ||
| + | {{ABSTRACT_PUBMED_21134641}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/CABP1_HUMAN CABP1_HUMAN]] Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).<ref>PMID:11865310</ref> <ref>PMID:14570872</ref> <ref>PMID:15140941</ref> <ref>PMID:15980432</ref> <ref>PMID:15895247</ref> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3ox6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX6 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021134641</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Findeisen, F.]] | [[Category: Findeisen, F.]] | ||
| Line 31: | Line 18: | ||
[[Category: Calcium-sensor]] | [[Category: Calcium-sensor]] | ||
[[Category: Ef-hand]] | [[Category: Ef-hand]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:58:21 2010'' | ||
Revision as of 08:29, 2 May 2013
Contents |
Crystal Structure of the calcium sensor calcium-binding protein 1 (CaBP1)
Template:ABSTRACT PUBMED 21134641
Function
[CABP1_HUMAN] Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).[1] [2] [3] [4] [5]
About this Structure
3ox6 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Findeisen F, Minor DL Jr. Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation. Structure. 2010 Dec 8;18(12):1617-31. PMID:21134641 doi:10.1016/j.str.2010.09.012
- ↑ Lee A, Westenbroek RE, Haeseleer F, Palczewski K, Scheuer T, Catterall WA. Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1. Nat Neurosci. 2002 Mar;5(3):210-7. PMID:11865310 doi:10.1038/nn805
- ↑ Haynes LP, Tepikin AV, Burgoyne RD. Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling. J Biol Chem. 2004 Jan 2;279(1):547-55. Epub 2003 Oct 21. PMID:14570872 doi:10.1074/jbc.M309617200
- ↑ Zhou H, Kim SA, Kirk EA, Tippens AL, Sun H, Haeseleer F, Lee A. Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels. J Neurosci. 2004 May 12;24(19):4698-708. PMID:15140941 doi:10.1523/JNEUROSCI.5523-03.2004
- ↑ Zhou H, Yu K, McCoy KL, Lee A. Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1. J Biol Chem. 2005 Aug 19;280(33):29612-9. Epub 2005 Jun 26. PMID:15980432 doi:M504167200
- ↑ Kinoshita-Kawada M, Tang J, Xiao R, Kaneko S, Foskett JK, Zhu MX. Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes. Pflugers Arch. 2005 Aug;450(5):345-54. Epub 2005 May 14. PMID:15895247 doi:10.1007/s00424-005-1419-1
