Bioinformatics analysis of interaction domain between NS4B protein and OCIAD2 protein

WANG Qianruo; GUO Fenglin; XU Jing; XU Ahui; GUO Yunli; KONG Lingbao

doi:10.3969/j.issn.1002-266X.2017.35.002

Abstract：Objective To analyze the interaction domains between nonstructural protein 4B (NS4B)protein and ovar-ian cancer immuno - reactive antigen domain containing 2 (OCIAD2)protein. Methods Transmembrane regions and lin-ear motifs were identified by searching the homepage of NCBI (National Biotechnology Information Center)for NS4B pro-tein and OCIAD2 protein GenBank sequence numbers,entering the UniPort (universal protein)home page to input the NS4B protein and OCIAD2 protein sequence numbers obtained in NCBI and to get the OCIAD2 protein number A4GSN1 and OCIAD2 protein number Q56VL3 in UniPort,and then entering the ELM home page to input the NS4B protein number A4GSN1 and the OCIAD2 protein number Q56VL3. Total interaction domains were sought by going to the ELM home page and selecting ELM binding domains. The protein transmembrane regions and the low-complexity regions were identified by entering the SMART home page and entering the protein sequence number,or protein sequence. Low-complexity regions exhibited an elastic structure that readily served as a domain for binding other proteins. Different transmembrane regions bond together because of their colocalization in the cell membrane. Results Transmembrane region was present in NS4B protein,but not in OCIAD2 protein. No linear interaction motif between NS4B protein and OCIAD2 protein was identified. OCIAD2 protein had a low-complexity region (88-98 amino acids). NS4B protein had two low complexity regions [(106-132 amino acids)and (141-154 amino acids)]. Conclusion OCIAD2 protein and NS4B protein may interact directly through low-complexity regions.