3q4a
From Proteopedia
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{{STRUCTURE_3q4a| PDB=3q4a | SCENE= }} | {{STRUCTURE_3q4a| PDB=3q4a | SCENE= }} | ||
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===Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 peptide=== | ===Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 peptide=== | ||
| + | {{ABSTRACT_PUBMED_21454478}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/CHIP_MOUSE CHIP_MOUSE]] E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.<ref>PMID:21855799</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021454478</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021454478</ref><references group="xtra"/><references/> |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
[[Category: Wu, J W.]] | [[Category: Wu, J W.]] | ||
| + | [[Category: E3 ubiquitin ligase]] | ||
| + | [[Category: Ligase-transcription complex]] | ||
Revision as of 08:33, 8 May 2013
Contents |
Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 peptide
Template:ABSTRACT PUBMED 21454478
Function
[CHIP_MOUSE] E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.[1]
About this Structure
3q4a is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Wang L, Liu YT, Hao R, Chen L, Chang Z, Wang HR, Wang ZX, Wu JW. Molecular Mechanism of the Negative Regulation of Smad1/5 Protein by Carboxyl Terminus of Hsc70-interacting Protein (CHIP). J Biol Chem. 2011 May 6;286(18):15883-94. Epub 2011 Mar 16. PMID:21454478 doi:10.1074/jbc.M110.201814
- ↑ Scaglione KM, Zavodszky E, Todi SV, Patury S, Xu P, Rodriguez-Lebron E, Fischer S, Konen J, Djarmati A, Peng J, Gestwicki JE, Paulson HL. Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP. Mol Cell. 2011 Aug 19;43(4):599-612. doi: 10.1016/j.molcel.2011.05.036. PMID:21855799 doi:10.1016/j.molcel.2011.05.036
