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4f0z
From Proteopedia
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{{STRUCTURE_4f0z| PDB=4f0z | SCENE= }} | {{STRUCTURE_4f0z| PDB=4f0z | SCENE= }} | ||
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===Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L=== | ===Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L=== | ||
| + | {{ABSTRACT_PUBMED_23468591}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN]] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref><ref>PMID:18838687</ref> [[http://www.uniprot.org/uniprot/VF238_ASFM2 VF238_ASFM2]] Inhibits activation of the NF-kappa-B transcription factor by preventing binding of NF-kappa-B subunits RELA and NFKB3 to DNA. Inhibits also the activity of the calcium/calmodulin-regulated phosphatase calcineurin (By similarity). [[http://www.uniprot.org/uniprot/CANB1_HUMAN CANB1_HUMAN]] Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. | ||
==About this Structure== | ==About this Structure== | ||
[[4f0z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/African_swine_fever_virus_malawi_lil_20/1 African swine fever virus malawi lil 20/1] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Z OCA]. | [[4f0z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/African_swine_fever_virus_malawi_lil_20/1 African swine fever virus malawi lil 20/1] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Z OCA]. | ||
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| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: African swine fever virus malawi lil 20/1]] | [[Category: African swine fever virus malawi lil 20/1]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 07:49, 27 March 2013
Contents |
Crystal Structure of Calcineurin in Complex with the Calcineurin-Inhibiting Domain of the African Swine Fever Virus Protein A238L
Template:ABSTRACT PUBMED 23468591
Function
[PP2BA_HUMAN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.[1][2] [VF238_ASFM2] Inhibits activation of the NF-kappa-B transcription factor by preventing binding of NF-kappa-B subunits RELA and NFKB3 to DNA. Inhibits also the activity of the calcium/calmodulin-regulated phosphatase calcineurin (By similarity). [CANB1_HUMAN] Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
About this Structure
4f0z is a 3 chain structure with sequence from African swine fever virus malawi lil 20/1 and Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Wang Y, Shibasaki F, Mizuno K. Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J Biol Chem. 2005 Apr 1;280(13):12683-9. Epub 2005 Jan 24. PMID:15671020 doi:M411494200
- ↑ Cereghetti GM, Stangherlin A, Martins de Brito O, Chang CR, Blackstone C, Bernardi P, Scorrano L. Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15803-8. doi:, 10.1073/pnas.0808249105. Epub 2008 Oct 6. PMID:18838687 doi:10.1073/pnas.0808249105
Categories: African swine fever virus malawi lil 20/1 | Homo sapiens | Phosphoprotein phosphatase | Grigoriu, S. | Page, R. | Peti, W. | Calcineurin inhibition | Calcium signaling | Calmodulin | Ef-hand | Heart | Hydrolase-protein binding complex | Ion channel | Lxvp | Nfat | Nucleus | Phosphatase | Pxixit | Rcan | Skeletal muscle | T-cell activation | Transcription regulation
