EVALUATION OF STRUCTURAL HOMOLOGY BETWEEN FUNCTIONALLY SIMILAR PROTEINS OF HIGHLY SPECIALIZED TISSUES ON THE EXAMPLE OF PROTEOGLYCANS AND SURFACTANT PROTEINS

Abstract

Proteins synthesized by cells of various tissues may have common functions, but at the same time have a heterologous structure. Previously, it was experimentally confirmed that lung suffractant proteins can be synthesized by chondrocytes of articular cartilage. Articular cartilage proteoglycans, such as lubricin (PRG4) and aggrecan (ACAN), have partially similar functions to surfactant proteins (SP-A, SP-B, SP-C, and SP-D). The main goal of the work was to evaluate of structural homology between these proteins. The Ugene program was the source of the of multiple and paired alignment results using the ClustalW and Smith–Waterman algorithm, and the MEGA11 program provided phylogenetic analysis. A common domain of the Lectin C-type family with a high degree of similarity to the domains of EGF-like proteoglycans (ACAN) and SMB 1 (PRG4) was found in ALAN, SP and SP-D proteins. The Sasposin domains of the SP-B protein had the greatest similarity with the PRG4 and ACAN domains over 57%. The BRICHOS domain of the SP-C protein had similarities with the SMB1, SMB2 (PRG4) and EGF-like (ACAN) domains. The mucin domain in the PRG4 structure was not detected. The phylogenetic analysis revealed about stidied proteins to have low level of evolution homology, as evidenced by bootstrap support.

Keywords

• multiple alignment
• clustalw
• prg4
• acan
• sp-a
• sp-b
• sp-c
• sp-d
• mucin
• articular cartilage
• множественное выравнивание
• clustalw
• prg4
• acan
• sp-a
• sp-b
• sp-c
• sp-d
• муцин
• суставной хрящ