Crystal structure of the PEG-bound SH3 domain of myosin IB from Entamoeba histolytica reveals its mode of ligand recognition

Gunjan Gautam, Syed Arif Abdul Rehman, Preeti Pandey, Samudrala Gourinath

Research output: Contribution to journalArticle (Academic Journal)peer-review

6 Citations (Scopus)


The versatility in the recognition of various interacting proteins by the SH3 domain drives a variety of cellular functions. Here, the crystal structure of the C-terminal SH3 domain of myosin IB from Entamoeba histolytica (EhMySH3) is reported at a resolution of 1.7 Å in native and PEG-bound states. Comparisons with other structures indicated that the PEG molecules occupy protein-protein interaction pockets similar to those occupied by the peptides in other peptide-bound SH3-domain structures. Also, analysis of the PEG-bound EhMySH3 structure led to the recognition of two additional pockets, apart from the conventional polyproline and specificity pockets, that are important for ligand interaction. Molecular-docking studies combined with various comparisons revealed structural similarity between EhMySH3 and the SH3 domain of β-Pix, and this similarity led to the prediction that EhMySH3 preferentially binds targets containing type II-like PXXP motifs. These studies expand the understanding of the EhMySH3 domain and provide extensive structural knowledge, which is expected to help in predicting the interacting partners which function together with myosin IB during phagocytosis in E. histolytica infections.

Original languageEnglish
Pages (from-to)672-682
Number of pages11
JournalActa Crystallographica Section D: Structural Biology
Issue numberPt 8
Publication statusPublished - 1 Aug 2017


  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Entamoeba histolytica/chemistry
  • Entamoebiasis/parasitology
  • Humans
  • Ligands
  • Molecular Docking Simulation
  • Myosin Type I/chemistry
  • Polyethylene Glycols/chemistry
  • Protein Binding
  • Protein Multimerization
  • Protozoan Proteins/chemistry
  • Sequence Alignment
  • src Homology Domains


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