OBJECTIVETo analyze the structure and function of PYGO1 protein with bioinformatics.

METHODSThe bioinformatic methods and tools were used to analyze the physical and chemical properties, transmembrane region, hydrophobicity and hyrdrophilicity, secondary structure and functional category of PYGO1 protein.

RESULTSThe bioinformatic analysis revealed that proline content was the highest of all amino acid residues in PYGO1 protein; the molecular formula was C(1943)H(2937)N(577)O(635)S(18) with a relative molecular mass of 45; and the theoretical isoelectric point was 6.38. The analysis also demonstrated that PYGO1 was a hydrophilic and non-transmembrane protein; its main component was alpha-helix and random coil; it contained a plant homeodomain.

CONCLUSIONHuman pygo1 gene may act as a transcription regulation factor to regulate the heart development and the progress of heart diseases.