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Nuclear protein PDB id
2je0
Jmol
Contents
Protein chains
(+ 0 more) 149 a.a. *
Ligands
GOL ×11
Waters ×307
* Residue conservation analysis
PDB id:
2je0
Name: Nuclear protein
Title: Crystal structure of pp32
Structure: Acidic leucine-rich nuclear phosphoprotein 32 fam member a. Chain: a, b, c, d, e, f. Fragment: lrr domain, residues 1-149. Synonym: potent heat-stable protein phosphatase 2a inhibito i1pp2a, acidic nuclear phosphoprotein pp32, leucine-rich a nuclear protein, lanp, putative hla-dr-associated protein phapi, mapmodulin, pp32. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.40Å     R-factor:   0.221     R-free:   0.269
Authors: T.Huyton,C.Wolberger
Key ref:
T.Huyton and C.Wolberger (2007). The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins. Protein Sci, 16, 1308-1315. PubMed id: 17567741 DOI: 10.1110/ps.072803507
Date:
12-Jan-07     Release date:   26-Jun-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P39687  (AN32A_HUMAN) -  Acidic leucine-rich nuclear phosphoprotein 32 family member A
Seq:
Struc: 		249 a.a.
149 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     protein binding     1 term  

 

 
DOI no: 10.1110/ps.072803507 Protein Sci 16:1308-1315 (2007)
PubMed id: 17567741  
 
 
The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins.
T.Huyton, C.Wolberger.
 
  ABSTRACT  
 
The tumor suppressor protein pp32 is highly overexpressed in many cancers of the breast and prostate, and has also been implicated in the neurodegenerative disease spinocerebellar ataxias type 1 (SCA1). Pp32 is a multifunctional protein that is involved in the regulation of transcription, apoptosis, phosphorylation, and cell cycle progression, the latter through its association with the hyperphosphorylated form of the retinoblastoma tumor suppressor. We have determined the structure of an N-terminal pp32 fragment comprising a capped leucine-rich repeat (LRR) domain, which provides insight into the structural and biochemical properties of the pp32 (Anp32) family of proteins.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Stereo ribbon representation of the structure of pp32DCT illustrating the canonical curved structure of the LRR domain.
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1308-1315) copyright 2007.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19452560 K.L.Hindle, J.Bella, and S.C.Lovell (2009).
Quantitative analysis and prediction of curvature in leucine-rich repeat proteins.
  Proteins, 77, 342-358.  
18410380 C.de Chiara, R.P.Menon, and A.Pastore (2008).
Structural bases for recognition of Anp32/LANP proteins.
  FEBS J, 275, 2548-2560.
PDB code: 2jqd
18156467 N.Courtemanche, and D.Barrick (2008).
Folding thermodynamics and kinetics of the leucine-rich repeat domain of the virulence factor Internalin B.
  Protein Sci, 17, 43-53.  
18462675 N.Courtemanche, and D.Barrick (2008).
The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway.
  Structure, 16, 705-714.  
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.