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・ Thiocyanate isomerase
・ Thiocyanatoiron
・ Thiocyanic acid
・ Thiocyanogen
・ Thiodia
・ Thiodia citrana
・ Thiodia glandulosana
・ Thiodia lerneana
・ Thiodia torridana
・ Thiodiglycol
・ Thiodina
・ Thiodiodes
・ Thioenol
・ Thioescaline
・ Thioester
Thioester-containing protein 1
・ Thioesterase
・ Thioethanolamine S-acetyltransferase
・ Thioether
・ Thioether S-methyltransferase
・ Thiofanox
・ Thiofentanyl
・ Thioflavin
・ Thiofrid of Echternach
・ Thioglycolate broth
・ Thioglycolic acid
・ Thiognatha
・ Thiognatha mameti
・ Thiognatha metachalca
・ Thioindigo


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Thioester-containing protein 1 : ウィキペディア英語版
Thioester-containing protein 1

Thioester containing protein 1, often simply referred to as TEP1 is a key component of the arthropod innate immune system. TEP1 was first identified as a key immunity gene in 2001 through functional studies on ''Anopheles gambiae'' mosquitoes.
TEP1 is an antimicrobial protein which acts in a system reminiscent of the human complement pathway, which damages the cell membranes of pathogens. Studies have shown that TEP1 is structurally and functionally homologous to the human complement protein C3. TEP1 is now known to be important in the resistance of ''Anopheles'' mosquitoes to ''Plasmodium'' infection, targeting the malaria parasite during its invasion into the mosquitoes body cavity. Following this discovery insect thioester containing proteins have come under increased scrutiny from the scientific community as possible targets for disease control.
TEP1 is coded for by two different alleles TEP1-S and TEP-R which are specific to susceptible and resistant mosquito populations respectively.
== Structure ==

Several crystallography studies have been used to determine the structure of TEP1. TEP1 contains a highly reactive thioester motif, which can undergo spontaneous hydrolysis. The thioester group is functionally essential for TEP1 to covalently bind to the surface of invading pathogens.〔 Tep1 is a multimeric protein, meaning it is formed of multiple associated polypetide chains. TEP1 is composed of a series of 6 macroglobulin domains, a β sheet CUB domain and an essential thioester domain, which protects the thioester motif from premature activation and hydrolysis by shielding it in the core of the molecule.
Comparisons of the TEP1-S and TEP1-R gene products show that the two allelic variants encode structural differences which are particularly prevalent in the thioester domain. These differences alter both the stability of the thioester bond and the ability of TEP1 to interact with other factors in the hemolymph of the mosquito.〔

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