3l82
From Proteopedia
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{{STRUCTURE_3l82| PDB=3l82 | SCENE= }} | {{STRUCTURE_3l82| PDB=3l82 | SCENE= }} | ||
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===X-ray Crystal structure of TRF1 and Fbx4 complex=== | ===X-ray Crystal structure of TRF1 and Fbx4 complex=== | ||
| + | {{ABSTRACT_PUBMED_20159592}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref> [[http://www.uniprot.org/uniprot/FBX4_HUMAN FBX4_HUMAN]] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.<ref>PMID:10531035</ref> <ref>PMID:16275645</ref> <ref>PMID:18598945</ref> <ref>PMID:20159592</ref> <ref>PMID:20181953</ref> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3l82]] is a 2 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=3L82 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020159592</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
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[[Category: Yang, Y T.]] | [[Category: Yang, Y T.]] | ||
[[Category: Zeng, Z X.]] | [[Category: Zeng, Z X.]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Adp-ribosylation]] | [[Category: Adp-ribosylation]] | ||
| - | [[Category: Alternative splicing]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Cell division]] | [[Category: Cell division]] | ||
[[Category: Chromosomal protein]] | [[Category: Chromosomal protein]] | ||
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[[Category: Cytoskeleton]] | [[Category: Cytoskeleton]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
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[[Category: Trfh domain]] | [[Category: Trfh domain]] | ||
[[Category: Ubl conjugation pathway]] | [[Category: Ubl conjugation pathway]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 10 13:46:43 2010'' | ||
Revision as of 20:44, 4 April 2013
Contents |
X-ray Crystal structure of TRF1 and Fbx4 complex
Template:ABSTRACT PUBMED 20159592
Function
[TERF1_HUMAN] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.[1] [FBX4_HUMAN] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.[2] [3] [4] [5] [6]
About this Structure
3l82 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Zeng Z, Wang W, Yang Y, Chen Y, Yang X, Diehl JA, Liu X, Lei M. Structural basis of selective ubiquitination of TRF1 by SCFFbx4. Dev Cell. 2010 Feb 16;18(2):214-25. PMID:20159592 doi:10.1016/j.devcel.2010.01.007
- ↑ de Lange T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 2005 Sep 15;19(18):2100-10. PMID:16166375 doi:10.1101/gad.1346005
- ↑ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M. Identification of a family of human F-box proteins. Curr Biol. 1999 Oct 21;9(20):1177-9. PMID:10531035 doi:S0960-9822(00)80020-2
- ↑ Lee TH, Perrem K, Harper JW, Lu KP, Zhou XZ. The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance. J Biol Chem. 2006 Jan 13;281(2):759-68. Epub 2005 Nov 7. PMID:16275645 doi:10.1074/jbc.M509855200
- ↑ Barbash O, Zamfirova P, Lin DI, Chen X, Yang K, Nakagawa H, Lu F, Rustgi AK, Diehl JA. Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer. Cancer Cell. 2008 Jul 8;14(1):68-78. doi: 10.1016/j.ccr.2008.05.017. PMID:18598945 doi:10.1016/j.ccr.2008.05.017
- ↑ Zeng Z, Wang W, Yang Y, Chen Y, Yang X, Diehl JA, Liu X, Lei M. Structural basis of selective ubiquitination of TRF1 by SCFFbx4. Dev Cell. 2010 Feb 16;18(2):214-25. PMID:20159592 doi:10.1016/j.devcel.2010.01.007
- ↑ Li Y, Hao B. Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase. J Biol Chem. 2010 Apr 30;285(18):13896-906. Epub 2010 Feb 24. PMID:20181953 doi:10.1074/jbc.M110.111518
Categories: Homo sapiens | Chen, Y. | Diehl, J A. | Lei, M. | Liu, X D. | Wang, W. | Yang, X M. | Yang, Y T. | Zeng, Z X. | Adp-ribosylation | Cell cycle | Cell division | Chromosomal protein | Cytoskeleton | Dna-binding | Gtpase domain | Helix | Mitosis | Nucleus | Phosphoprotein | Telomere | Trfh domain | Ubl conjugation pathway
