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- W2374056996 abstract "BMP4 is known for its critical roles in embryonic development, mesenchymal development, organogenesis, and the initiation and progression of tumor. To know the functionally important residues and 3D structure of BMP protein will be helpful for understanding its function and its relationship with other proteins in the BMP signal pathway. The present study aims to identify some functionally important residues and its interaction with corresponding ligands of BMP4 protein. Here, a total of 100 non-redundant protein sequences of BMP4 from various mammals were retrieved from NCBI database. Of the 100 sequences, only 72 sequences were selected for multiple sequence alignment and the phylogenetic tree was split into 10 evenly distributed partitions, namely P1﹣P10 in order of evolutionary time cut-off(Fig.1). Based on these results, detailed analyses on the evolutionary conservation information were performed through a variety of bioinformatics tools. Conservative analyses show that the TGFβ-propeptide domain contains 22 highly conservative residues. However, the TGF-β domain only contains 84 class-specific residues(Fig.3). To further explore the functional binding sites of BMP4 protein, the ligand-binding pockets were predicted using software Meta Pocket 2.0. The results show that there exist three binding sites and the ligand-binding sites are surrounded the pockets(Fig.4). This study will provide useful information for identifying key residues from functional regions and predicting unknown functional sites in BMP4 family." @default.
- W2374056996 created "2016-06-24" @default.
- W2374056996 creator A5009369536 @default.
- W2374056996 date "2015-01-01" @default.
- W2374056996 modified "2023-09-24" @default.
- W2374056996 title "Evolutionary Trace Analysis of Functional Sites of the BMP4" @default.
- W2374056996 hasPublicationYear "2015" @default.
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