Structural And Functional Bioinformatics Analysis Of Netrin-1 Protein

Objective:The Netrin-1 protein is a potential tumor diagnosis and treatment target,but its structural features and cancer-promoting mechanisms have not yet been fully elucidated.In this paper,the bioinformatics method is used to comprehensively predict and analyze the structure and function of the Netrin-1 protein,which provides a theoretical basis for cancer pathogenesis and treatment.Methods:The protein sequence of Netrin-1 is searched by UniProt,and the physicochemical properties and hydrophilicity/hydrophobicity of human Netrin-1 protein are predicted by the ProtParam database and DNAMAN software.Subcellular localization of human Netrin-1 protein is analyzed by Genecards database,spatial structure of human Netrin-1 protein is analyzed by SOPMA and PDB databases,and basic structure of human Netrin-1 protein is analyzed by UniProt and NCBI Conserved Domain database,homologous sequence comparison and evolution relationship of human Netrin-1 protein and chimpanzee?H2QC90?,mouse?O09118?,rat?Q924Z9?,cow?F1N0C7?,dog?F1PSP7?,chicken?Q90922?,lizard?G1KUB3?,zebrafish?O42203?,tetraodon?H3CIU4?Netrin-1 proteins are analyzed by ClustalX2.1 and DNAMAN software.the phosphorylation and acetylation of human Netrin-1 protein are analyzed by GPS3.0 and GPS PAIL2.0 software,GO analysis,pathway analysis and interaction protein analysis of human Netrin-1 protein are by AmiGO2,KEGG and String online databases,protein expression profiling of human Netrin-1 protein is analyzed by THE HUMAN PROTEIN ATLAS database.Results:The human Netrin-1 protein is composed of VI,V-1,V-2,V-3 and NTR domains and contains 604 amino acids.The total molecular formula is C₂₉₂₅H₄₆₀₉N₈₉₁O₈₆₆S₅₁,the total number of atoms is 9342,and the molecular mass is67748.28,which is highly conserved during evolution.It belongs to the NTR_like superfamily and the Laminin_N superfamily and it is a hydrophilic and unstable secreted protein whose V-1,V-2 and V-3 domains are the most conservative.The main secondary structure of the protein is 64.57%of random coils,and the remaining extended chain,?-helix and?-sheet account for 18.38%,12.58%,and 4.47%,respectively.There are more potential phosphorylation sites in the VI domain and the V-1,V-2,V-3 domains,while the acetylation sites are mainly concentrated at the end of the NTR domain.The interaction proteins are in addition to the classic DCC,UNC5A,UNC5B,UNC5C,UNC5D,NEO1 and DSCAM,as well as FYN,BCAR1,MAP1B,etc.It is highly expressed in solid tumors such as colon cancer,breast cancer,and prostate cancer.Conclusions:The structural and functional information of Netrin-1 protein is combined,suggesting that it may promote the malignant progression of tumor by regulating a variety of tumor-related signaling pathways.