1fbv
From Proteopedia
(New page: 200px<br /> <applet load="1fbv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbv, resolution 2.9Å" /> '''STRUCTURE OF A CBL-U...) |
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| - | [[Image:1fbv.gif|left|200px]]<br /> | + | [[Image:1fbv.gif|left|200px]]<br /><applet load="1fbv" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fbv" size=" | + | |
caption="1fbv, resolution 2.9Å" /> | caption="1fbv, resolution 2.9Å" /> | ||
'''STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES'''<br /> | '''STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by | + | Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by mediating protein ubiquitination. The c-Cbl proto-oncogene is a RING family E3 that recognizes activated receptor tyrosine kinases, promotes their ubiquitination by a ubiquitin-conjugating enzyme (E2) and terminates signaling. The crystal structure of c-Cbl bound to a cognate E2 and a kinase peptide shows how the RING domain recruits the E2. A comparison with a HECT family E3-E2 complex indicates that a common E2 motif is recognized by the two E3 families. The structure reveals a rigid coupling between the peptide binding and the E2 binding domains and a conserved surface channel leading from the peptide to the E2 active site, suggesting that RING E3s may function as scaffolds that position the substrate and the E2 optimally for ubiquitin transfer. |
==About this Structure== | ==About this Structure== | ||
| - | 1FBV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http:// | + | 1FBV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
| - | [[Category: Jeffrey, P | + | [[Category: Jeffrey, P D.]] |
| - | [[Category: Pavletich, N | + | [[Category: Pavletich, N P.]] |
[[Category: Wang, P.]] | [[Category: Wang, P.]] | ||
[[Category: Zheng, N.]] | [[Category: Zheng, N.]] | ||
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[[Category: zap-70]] | [[Category: zap-70]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:03 2008'' |
Revision as of 10:37, 21 February 2008
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STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION IN UBIQUITIN-PROTEIN LIGASES
Overview
Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by mediating protein ubiquitination. The c-Cbl proto-oncogene is a RING family E3 that recognizes activated receptor tyrosine kinases, promotes their ubiquitination by a ubiquitin-conjugating enzyme (E2) and terminates signaling. The crystal structure of c-Cbl bound to a cognate E2 and a kinase peptide shows how the RING domain recruits the E2. A comparison with a HECT family E3-E2 complex indicates that a common E2 motif is recognized by the two E3 families. The structure reveals a rigid coupling between the peptide binding and the E2 binding domains and a conserved surface channel leading from the peptide to the E2 active site, suggesting that RING E3s may function as scaffolds that position the substrate and the E2 optimally for ubiquitin transfer.
About this Structure
1FBV is a Protein complex structure of sequences from Homo sapiens with and as ligands. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases., Zheng N, Wang P, Jeffrey PD, Pavletich NP, Cell. 2000 Aug 18;102(4):533-9. PMID:10966114
Page seeded by OCA on Thu Feb 21 12:37:03 2008
Categories: Homo sapiens | Protein complex | Ubiquitin--protein ligase | Jeffrey, P D. | Pavletich, N P. | Wang, P. | Zheng, N. | SO4 | ZN | Cbl | E2 | E3 | Phosphorylation | Protein degradation | Tyrosine kinase | Ubch7 | Ubiquitin | Ubiquitination | Zap-70
