3kov: Difference between revisions
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{{STRUCTURE_3kov| PDB=3kov | SCENE= }} | {{STRUCTURE_3kov| PDB=3kov | SCENE= }} | ||
===Structure of MEF2A bound to DNA reveals a completely folded MADS-box/MEF2 domain that recognizes DNA and recruits transcription co-factors=== | ===Structure of MEF2A bound to DNA reveals a completely folded MADS-box/MEF2 domain that recognizes DNA and recruits transcription co-factors=== | ||
{{ABSTRACT_PUBMED_20132824}} | |||
==Disease== | |||
[[http://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN]] Defects in MEF2A are a cause of coronary artery disease, autosomal dominant, type 1 (ADCAD1) [MIM:[http://omim.org/entry/608320 608320]]. A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction. | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/MEF2A_HUMAN MEF2A_HUMAN]] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation.<ref>PMID:9858528</ref><ref>PMID:11904443</ref><ref>PMID:12691662</ref><ref>PMID:15834131</ref><ref>PMID:16563226</ref><ref>PMID:16371476</ref><ref>PMID:16484498</ref> | |||
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==About this Structure== | ==About this Structure== | ||
[[3kov]] is a 8 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=3KOV OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020132824</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
Line 32: | Line 22: | ||
[[Category: Wu, Y.]] | [[Category: Wu, Y.]] | ||
[[Category: Ye, J.]] | [[Category: Ye, J.]] | ||
[[Category: Activator]] | [[Category: Activator]] | ||
[[Category: Apoptosis]] | [[Category: Apoptosis]] | ||
[[Category: Developmental protein]] | [[Category: Developmental protein]] | ||
Line 51: | Line 39: | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
[[Category: Transcription-dna complex]] | [[Category: Transcription-dna complex]] | ||
Revision as of 04:22, 25 March 2013
Structure of MEF2A bound to DNA reveals a completely folded MADS-box/MEF2 domain that recognizes DNA and recruits transcription co-factorsStructure of MEF2A bound to DNA reveals a completely folded MADS-box/MEF2 domain that recognizes DNA and recruits transcription co-factors
Template:ABSTRACT PUBMED 20132824
DiseaseDisease
[MEF2A_HUMAN] Defects in MEF2A are a cause of coronary artery disease, autosomal dominant, type 1 (ADCAD1) [MIM:608320]. A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction.
FunctionFunction
[MEF2A_HUMAN] Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation.[1][2][3][4][5][6][7]
About this StructureAbout this Structure
3kov is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Wu Y, Dey R, Han A, Jayathilaka N, Philips M, Ye J, Chen L. Structure of the MADS-box/MEF2 domain of MEF2A bound to DNA and its implication for myocardin recruitment. J Mol Biol. 2010 Mar 26;397(2):520-33. Epub 2010 Feb 2. PMID:20132824 doi:10.1016/j.jmb.2010.01.067
- ↑ Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J. Regulation of the MEF2 family of transcription factors by p38. Mol Cell Biol. 1999 Jan;19(1):21-30. PMID:9858528
- ↑ Okamoto S, Li Z, Ju C, Scholzke MN, Mathews E, Cui J, Salvesen GS, Bossy-Wetzel E, Lipton SA. Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3974-9. PMID:11904443 doi:10.1073/pnas.022036399
- ↑ Gong X, Tang X, Wiedmann M, Wang X, Peng J, Zheng D, Blair LA, Marshall J, Mao Z. Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis. Neuron. 2003 Apr 10;38(1):33-46. PMID:12691662
- ↑ Zhu B, Ramachandran B, Gulick T. Alternative pre-mRNA splicing governs expression of a conserved acidic transactivation domain in myocyte enhancer factor 2 factors of striated muscle and brain. J Biol Chem. 2005 Aug 5;280(31):28749-60. Epub 2005 Apr 15. PMID:15834131 doi:10.1074/jbc.M502491200
- ↑ Riquelme C, Barthel KK, Liu X. SUMO-1 modification of MEF2A regulates its transcriptional activity. J Cell Mol Med. 2006 Jan-Mar;10(1):132-44. PMID:16563226
- ↑ Hietakangas V, Anckar J, Blomster HA, Fujimoto M, Palvimo JJ, Nakai A, Sistonen L. PDSM, a motif for phosphorylation-dependent SUMO modification. Proc Natl Acad Sci U S A. 2006 Jan 3;103(1):45-50. Epub 2005 Dec 21. PMID:16371476 doi:10.1073/pnas.0503698102
- ↑ Shalizi A, Gaudilliere B, Yuan Z, Stegmuller J, Shirogane T, Ge Q, Tan Y, Schulman B, Harper JW, Bonni A. A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation. Science. 2006 Feb 17;311(5763):1012-7. PMID:16484498 doi:10.1126/science.1122513
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Homo sapiens
- Chen, L.
- Dey, R.
- Han, A.
- Jayathilaka, N.
- Philips, M.
- Wu, Y.
- Ye, J.
- Activator
- Apoptosis
- Developmental protein
- Differentiation
- Disease mutation
- Dna-binding
- Isopeptide bond
- Mads-box/mef2 domain
- Neurogenesis
- Nucleus
- Phosphoprotein
- Protein-dna complex
- Protein-protein docking
- Transcription
- Transcription co-factor
- Transcription regulation
- Transcription-dna complex