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4gba

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Revision as of 03:44, 25 December 2014

DCNL complex with N-terminally acetylated NEDD8 E2 peptide

Structural highlights

4gba is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4gao
Gene:	DCUN1D3 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DCNL3_HUMAN] Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8-conjugating E2 enzyme UBE2F. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.^[1] [UBE2F_HUMAN] Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.

Publication Abstract from PubMed

Little is known about molecular recognition of acetylated N termini, despite prevalence of this modification among eukaryotic cytosolic proteins. We report that the family of human DCN-like (DCNL) co-E3s, which promote ligation of the ubiquitin-like protein NEDD8 to cullin targets, recognizes acetylated N termini of the E2 enzymes UBC12 and UBE2F. Systematic biochemical and biophysical analyses reveal 40- and 10-fold variations in affinities among different DCNL-cullin and DCNL-E2 complexes, contributing to varying efficiencies of different NEDD8 ligation cascades. Structures of DCNL2 and DCNL3 complexes with N-terminally acetylated peptides from UBC12 and UBE2F illuminate a common mechanism by which DCNL proteins recognize N-terminally acetylated E2s and how selectivity for interactions dependent on N-acetyl-methionine are established through side chains recognizing distal residues. Distinct preferences of UBC12 and UBE2F peptides for inhibiting different DCNLs, including the oncogenic DCNL1 protein, suggest it may be possible to develop small molecules blocking specific N-acetyl-methionine-dependent protein interactions.

Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes.,Monda JK, Scott DC, Miller DJ, Lydeard J, King D, Harper JW, Bennett EJ, Schulman BA Structure. 2012 Nov 27. pii: S0969-2126(12)00409-1. doi:, 10.1016/j.str.2012.10.013. PMID:23201271^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Monda JK, Scott DC, Miller DJ, Lydeard J, King D, Harper JW, Bennett EJ, Schulman BA. Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes. Structure. 2012 Nov 27. pii: S0969-2126(12)00409-1. doi:, 10.1016/j.str.2012.10.013. PMID:23201271 doi:http://dx.doi.org/10.1016/j.str.2012.10.013
↑ Monda JK, Scott DC, Miller DJ, Lydeard J, King D, Harper JW, Bennett EJ, Schulman BA. Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes. Structure. 2012 Nov 27. pii: S0969-2126(12)00409-1. doi:, 10.1016/j.str.2012.10.013. PMID:23201271 doi:http://dx.doi.org/10.1016/j.str.2012.10.013

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gba"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gba RCSB], [http://www.ebi.ac.uk/pdbsum/4gba PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DCNL3_HUMAN DCNL3_HUMAN]] Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8-conjugating E2 enzyme UBE2F. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.<ref>PMID:23201271</ref>  [[http://www.uniprot.org/uniprot/UBE2F_HUMAN UBE2F_HUMAN]] Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4gba

From Proteopedia

Revision as of 03:44, 25 December 2014

DCNL complex with N-terminally acetylated NEDD8 E2 peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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