Protein structure analysis and molecular evolution of CD34 in Homo sapiens

CD34 is a kind of highly glycosylated type I transmembrane glycoprotein,selectively present on hematopoietic cells, endothelial progenitor cells, mast cells within the human body or other animals. It is related to the transportation and setting of the hematogenic stem cells, intercellular adhesion, the lymphocyte homing and some pathological phenomenons. The amino acid sequence of CD34 was obtained from NCBI and analyzed by using different bioinformatics software tools and Internet resources for better understanding of the expression and regulation of CD34. Based on some investigations we know that CD34 is a stable hydrophilic membrane protein and own a structure with transmembrane domain. The secondary structure is composed of alpha helix (23.12%), extended strand (16.62%) and random coil (60.26%). The molecular evolution analysis revealed that the 7 species were divided into two major branches. One is for Mus sp, Homo sapiens, Callithrix jacchus and the other is Capra hircus, Bos Taurus,Tursiops truncates, Felis catus. This phylogenetic tree is consistent well with recognized evolutionary relationship among these species. In this article the main focus will be on the physicochemical properties, structures and functions of CD34 in human and the evolutionary relationship with different organisms.