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PDBsum entry 2lb0
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Signaling protein/transcription
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PDB id
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2lb0
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PDB id:
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| Name: |
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Signaling protein/transcription
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Title:
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Structure of the first ww domain of human smurf1 in complex with a di- phosphorylated human smad1 derived peptide
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Structure:
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E3 ubiquitin-protein ligase smurf1. Chain: a. Fragment: residues 235-267. Synonym: hsmurf1, smad ubiquitination regulatory factor 1, smad- specific e3 ubiquitin-protein ligase 1. Engineered: yes. Mothers against decapentaplegic homolog 1. Chain: b. Fragment: residues 208-217.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: smurf1, kiaa1625. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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NMR struc:
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21 models
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Authors:
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M.J.Macias,E.Aragon,N.Goerner,A.Zaromytidou,Q.Xi,A.Escobedo, J.Massague
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Key ref:
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E.Aragón
et al.
(2011).
A Smad action turnover switch operated by WW domain readers of a phosphoserine code.
Genes Dev,
25,
1275-1288.
PubMed id:
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Date:
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22-Mar-11
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Release date:
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06-Jul-11
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PROCHECK
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Headers
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References
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Q9HCE7
(SMUF1_HUMAN) -
E3 ubiquitin-protein ligase SMURF1 from Homo sapiens
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Seq:
Struc:
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757 a.a.
33 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.2.3.2.26
- HECT-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Genes Dev
25:1275-1288
(2011)
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PubMed id:
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A Smad action turnover switch operated by WW domain readers of a phosphoserine code.
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E.Aragón,
N.Goerner,
A.I.Zaromytidou,
Q.Xi,
A.Escobedo,
J.Massagué,
M.J.Macias.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Massagué
(2012).
TGFβ signalling in context.
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Nat Rev Mol Cell Biol,
13,
616-630.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
