1wd2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1wd2.jpg|left|200px]]< | [[Image:1wd2.jpg|left|200px]] | ||
'''Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif''' | {{Structure | ||
|PDB= 1wd2 |SIZE=350|CAPTION= <scene name='initialview01'>1wd2</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1WD2 is a [ | 1WD2 is a [[Single protein]] structure of 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=1WD2 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING., Capili AD, Edghill EL, Wu K, Borden KL, J Mol Biol. 2004 Jul 23;340(5):1117-29. PMID:[http:// | Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING., Capili AD, Edghill EL, Wu K, Borden KL, J Mol Biol. 2004 Jul 23;340(5):1117-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15236971 15236971] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 27: | Line 36: | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:55:27 2008'' | ||
Revision as of 15:55, 20 March 2008
| |||||||
| Ligands: | |||||||
| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif
OverviewOverview
The really interesting new gene (RING) family of proteins contains over 400 members with diverse physiological functions. A subset of these domains is found in the context of the RING-IBR-RING/TRIAD motifs which function as E3 ubiquitin ligases. Our sequence analysis of the C-terminal RING (RING2) from this motif show that several metal ligating and hydrophobic residues critical for the formation of a classical RING cross-brace structure are not present. Thus, we determined the structure of the RING2 from the RING-IBR-RING motif of HHARI and showed that RING2 has a completely distinct topology from classical RINGs. Notably, RING2 binds only one zinc atom per monomer rather than two and uses a different hydrophobic network to that of classical RINGs. Additionally, this RING2 topology is novel, bearing slight resemblance to zinc-ribbon motifs around the zinc site and is different from the topologies of the zinc binding sites found in RING and PHDs. We demonstrate that RING2 acts as an E3 ligase in vitro and using mutational analysis deduce the structural features required for this activity. Further, mutations in the RING-IBR-RING of Parkin cause a rare form of Parkinsonism and these studies provide an explanation for those mutations that occur in its RING2. From a comparison of the RING2 structure with those reported for RINGs, we infer sequence determinants that allow discrimination between RING2 and RING domains at the sequence analysis level.
DiseaseDisease
Known disease associated with this structure: Schizophrenia, susceptibility to OMIM:[142445]
About this StructureAbout this Structure
1WD2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING., Capili AD, Edghill EL, Wu K, Borden KL, J Mol Biol. 2004 Jul 23;340(5):1117-29. PMID:15236971
Page seeded by OCA on Thu Mar 20 14:55:27 2008