spacer
spacer

PDBsum entry 2jup

Go to PDB code: 
protein ligands links
Transcription PDB id
2jup
Jmol
Contents
Protein chain
37 a.a. *
Ligands
GLY-PRO-PRO-LEU-
ILE-PRO-PRO-PRO-
PRO
* Residue conservation analysis
PDB id:
2jup
Name: Transcription
Title: Fbp28ww2 domain in complex with the pplipppp peptide
Structure: Transcription elongation regulator 1. Chain: w. Fragment: ww 2 domain, sequence database residues 430-466. Synonym: tata box-binding protein- associated factor 2s, transcription factor ca150, p144, formin- binding protein 28, fbp 28. Engineered: yes. Formin-1. Chain: p.
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: tcerg1, taf2s. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the authors state that the peptide was chemically synthesized and the sequence corresponds to the
NMR struc: 10 models
Authors: X.Ramirez-Espain,L.Ruiz,P.Martin-Malpartida,H.Oschkinat, M.J.Macias
Key ref:
X.Ramirez-Espain et al. (2007). Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains. J Mol Biol, 373, 1255-1268. PubMed id: 17915251 DOI: 10.1016/j.jmb.2007.08.052
Date:
01-Sep-07     Release date:   06-Nov-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8CGF7  (TCRG1_MOUSE) -  Transcription elongation regulator 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1100 a.a.
37 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/j.jmb.2007.08.052 J Mol Biol 373:1255-1268 (2007)
PubMed id: 17915251  
 
 
Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains.
X.Ramirez-Espain, L.Ruiz, P.Martin-Malpartida, H.Oschkinat, M.J.Macias.
 
  ABSTRACT  
 
Formin homology 1 (FH1), is a long proline-rich region of formins, shown to bind to five WW containing proteins named formin binding proteins (FBPs). FH1 has several potential binding regions but only the PPLPx motif and its interaction with FBP11WW1 has been characterized structurally. To detect whether additional motifs exist in FH1, we synthesized five peptides and investigated their interaction with FBP28WW2, FBP11WW1 and FBP11WW2 domains. Peptides of sequence PTPPPLPP (positive control), PPPLIPPPP and PPLIPPPP (new motifs) interact with the domains with micromolar affinity. We observed that FBP28WW2 and FBP11WW2 behave differently from FBP11WW1 in terms of motif selection and affinity, since they prefer a doubly interrupted proline stretch of sequence PPLIPP. We determined the NMR structure of three complexes involving the FBP28WW2 domain and the three ligands. Depending on the peptide under study, the domain interacts with two proline residues accommodated in either the XP or the XP2 groove. This difference represents a one-turn displacement of the domain along the ligand sequence. To understand what drives this behavior, we performed further structural studies with the FBP11WW1 and a mutant of FBP28WW2 mimicking the XP2 groove of FBP11WW1. Our observations suggest that the nature of the XP2 groove and the balance of flexibility/rigidity around loop 1 of the domain contribute to the selection of the final ligand positioning in fully independent domains. Additionally, we analyzed the binding of a double WW domain region, FBP11WW1-2, to a long stretch of FH1 using fluorescence spectroscopy and NMR titrations. With this we show that the presence of two consecutive WW domains may also influence the selection of the binding mode, particularly if both domains can interact with consecutive motifs in the ligand. Our results represent the first observation of protein-ligand recognition where a pair of WW and two consecutive motifs in a ligand participate simultaneously.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Solution structure of FBP28WW in complex with the PPPLIPPPP peptide. (a) Stereo view of the best-fit backbone (N, C^α, C′) superposition of the ten lowest energy structures after water refinement with the ligand (domain in blue and ligand in red). (b) Left: Surface representation of the lowest energy structure (ligand in brown). Right: Cartoon representation with the secondary structural elements of the domain shown in green, residues participating in contacts in dark yellow and ligand in brown.
Figure 5.
Figure 5. Solution structure of FBP28WW in complex with the PPLIPPPP peptide. (a) Stereo view of the best-fit backbone (N, C^α, C′) superposition of the ten lowest energy structures after water refinement with the ligand (domain in blue and ligand in red). (b) Left: Corresponding surface representation of the lowest energy structure (ligand in dark green). Right: Cartoon representation with the secondary structural elements of the domain shown in green, residues participating in contacts in dark yellow and ligand in dark green.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 373, 1255-1268) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20937913 P.A.Chong, H.Lin, J.L.Wrana, and J.D.Forman-Kay (2010).
Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity.
  Proc Natl Acad Sci U S A, 107, 18404-18409.
PDB code: 2kxq
19592703 X.Huang, M.Beullens, J.Zhang, Y.Zhou, E.Nicolaescu, B.Lesage, Q.Hu, J.Wu, M.Bollen, and Y.Shi (2009).
Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21).
  J Biol Chem, 284, 25375-25387.
PDB code: 2jxw
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. Where a reference describes a PDB structure, the PDB code is shown on the right.