1wd2: Difference between revisions

Revision as of 11:35, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wd2.png

Template:STRUCTURE 1wd2

Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motifSolution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif

Template:ABSTRACT PUBMED 15236971

About this StructureAbout this Structure

1WD2 is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1wd2|  PDB=1wd2  |  SCENE=  }}
-'''Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif'''
+===Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15236971}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15236971 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15236971}}
 ==About this Structure==
-WD2 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].
+WD2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WD2 OCA].
 ==Reference==
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 [[Category: Triad]]
 [[Category: Zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:29:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:34:52 2008''