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PDBsum entry 1zm0

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protein Protein-protein interface(s) links
Lipid binding protein PDB id
1zm0
Jmol
Contents
Protein chains
96 a.a. *
Waters ×163
* Residue conservation analysis
PDB id:
1zm0
Name: Lipid binding protein
Title: Crystal structure of the carboxyl terminal ph domain of pleckstrin to 2.1 angstroms
Structure: Pleckstrin. Chain: a, b. Fragment: ph2 domain. Synonym: platelet p47 protein. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: plek, p47. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.236     R-free:   0.244
Authors: S.G.Jackson,Y.Zhang,K.Zhang,R.Summerfield,R.J.Haslam, M.S.Junop
Key ref:
S.G.Jackson et al. (2006). Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 A. Acta Crystallogr D Biol Crystallogr, 62, 324-330. PubMed id: 16510979 DOI: 10.1107/S0907444905043179
Date:
09-May-05     Release date:   28-Feb-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08567  (PLEK_HUMAN) -  Pleckstrin
Seq:
Struc:
350 a.a.
96 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1107/S0907444905043179 Acta Crystallogr D Biol Crystallogr 62:324-330 (2006)
PubMed id: 16510979  
 
 
Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 A.
S.G.Jackson, Y.Zhang, X.Bao, K.Zhang, R.Summerfield, R.J.Haslam, M.S.Junop.
 
  ABSTRACT  
 
Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 A resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 The observed non-crystallographic C-PH dimer. The dimer interface is illustrated using a combination of ribbon and semi-transparent space-filling diagrams. A reciprocal interaction between the fifth -strand from one subunit and the -helix from the other forms the dimer interface. Subunits A and B are coloured blue and yellow, respectively.
Figure 6.
Figure 6 Stereoview of the structural comparison between the DAPP1 PH and C-PH ligand-binding pockets. DAPP1 PH is shown in gold using a combined ribbon/stick representation, while C-PH is shown in purple. Ins(1,3,4,5)P[4] observed in the DAPP1 structure is shown with C atoms in green, phosphate in orange and O atoms in red.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 324-330) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21310079 S.G.Jackson, S.Al-Saigh, C.Schultz, and M.S.Junop (2011).
Inositol pentakisphosphate isomers bind PH domains with varying specificity and inhibit phosphoinositide interactions.
  BMC Struct Biol, 11, 11.  
18034889 S.G.Jackson, Y.Zhang, R.J.Haslam, and M.S.Junop (2007).
Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate.
  BMC Struct Biol, 7, 80.
PDB codes: 2i5c 2i5f
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