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PDBsum entry 2lb3

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protein ligands links
Signaling protein/transcription PDB id
2lb3
Jmol
Contents
Protein chain
36 a.a.
Ligands
ILE-PRO-GLU-TPO-
PRO-PRO-PRO-GLY
PDB id:
2lb3
Name: Signaling protein/transcription
Title: Structure of the ww domain of pin1 in complex with a human phosphorylated smad3 derived peptide
Structure: Peptidyl-prolyl cis-trans isomerase nima-interact chain: a. Fragment: residues 6-41. Synonym: peptidyl-prolyl cis-trans isomerase pin1, ppiase p rotamase pin1. Engineered: yes. Mothers against decapentaplegic homolog 2. Chain: b. Fragment: residues 176-183.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pin1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
NMR struc: 20 models
Authors: M.J.Macias,E.Aragon,N.Goerner,A.Zaromytidou,Q.Xi,A.Escobedo, J.Massague
Key ref: 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: 21685363
Date:
22-Mar-11     Release date:   06-Jul-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Seq:
Struc:
163 a.a.
36 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Genes Dev 25:1275-1288 (2011)
PubMed id: 21685363  
 
 
A Smad action turnover switch operated by WW domain readers of a phosphoserine code.
E.Aragón, N.Goerner, A.I.Zaromytidou, Q.Xi, A.Escobedo, J.Massagué, M.J.Macias.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22992590 J.Massagué (2012).
TGFβ signalling in context.
  Nat Rev Mol Cell Biol, 13, 616-630.  
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.