西北民族大学学报:自然科学版
西北民族大學學報:自然科學版
서북민족대학학보:자연과학판
Journal of Northwest Minorities University:Natural Science Edition
2011年
2期
73-80,90
,共9页
欧阳霞辉%兰玉婷%赵有红%侯兰新%李春鸣
歐暘霞輝%蘭玉婷%趙有紅%侯蘭新%李春鳴
구양하휘%란옥정%조유홍%후란신%리춘명
雌激素相关受体%黑腹果蝇%致倦库蚊%埃及伊蚊%意大利蜜蜂%丽蝇蛹集金小蜂%蛋白质结构预测
雌激素相關受體%黑腹果蠅%緻倦庫蚊%埃及伊蚊%意大利蜜蜂%麗蠅蛹集金小蜂%蛋白質結構預測
자격소상관수체%흑복과승%치권고문%애급이문%의대리밀봉%려승용집금소봉%단백질결구예측
Estrogen-related receptor (ERR)%Drosophila melanogaster%Culex pipiens quinquefasciatus%Aedes aegypti%Apis mellifera%Nasonia vitripennis%Protein structure prediction
采用生物信息学的方法和工具对已在GenBaak上注册的黑腹果蝇(Drosophila melanogaster)、致倦库蚊(Culexpi piensquin quefasciatus)、埃及伊蚊(Aedes aegypti)、意大利蜜蜂(Apis mellifera)、丽蝇蛹集金小蜂(Nasonia vitripennis)的雌激素相关受体ERR的核酸及氨基酸序列进行分析,并对其组成成分、理化性质、疏水性/亲水性、蛋白质二级及三级结构、分子系统进化关系等进行了预测和推断.结果表明:昆虫ERR是一个亲水性蛋白.在ERR整体蛋白结构中α-螺旋和不规则卷曲是ERR最大量的结构元件,而β-折叠则散布于整个蛋白质中.ERR蛋白的DNA结合区(DID)主要由三个α-螺旋和三个β-折叠构成,包含两个锌指结构.配体结合区(LBD)主要由3个β-折叠和11个α-螺旋构成.
採用生物信息學的方法和工具對已在GenBaak上註冊的黑腹果蠅(Drosophila melanogaster)、緻倦庫蚊(Culexpi piensquin quefasciatus)、埃及伊蚊(Aedes aegypti)、意大利蜜蜂(Apis mellifera)、麗蠅蛹集金小蜂(Nasonia vitripennis)的雌激素相關受體ERR的覈痠及氨基痠序列進行分析,併對其組成成分、理化性質、疏水性/親水性、蛋白質二級及三級結構、分子繫統進化關繫等進行瞭預測和推斷.結果錶明:昆蟲ERR是一箇親水性蛋白.在ERR整體蛋白結構中α-螺鏇和不規則捲麯是ERR最大量的結構元件,而β-摺疊則散佈于整箇蛋白質中.ERR蛋白的DNA結閤區(DID)主要由三箇α-螺鏇和三箇β-摺疊構成,包含兩箇鋅指結構.配體結閤區(LBD)主要由3箇β-摺疊和11箇α-螺鏇構成.
채용생물신식학적방법화공구대이재GenBaak상주책적흑복과승(Drosophila melanogaster)、치권고문(Culexpi piensquin quefasciatus)、애급이문(Aedes aegypti)、의대리밀봉(Apis mellifera)、려승용집금소봉(Nasonia vitripennis)적자격소상관수체ERR적핵산급안기산서렬진행분석,병대기조성성분、이화성질、소수성/친수성、단백질이급급삼급결구、분자계통진화관계등진행료예측화추단.결과표명:곤충ERR시일개친수성단백.재ERR정체단백결구중α-라선화불규칙권곡시ERR최대량적결구원건,이β-절첩칙산포우정개단백질중.ERR단백적DNA결합구(DID)주요유삼개α-라선화삼개β-절첩구성,포함량개자지결구.배체결합구(LBD)주요유3개β-절첩화11개α-라선구성.
In the present study, estrogen- related receptors (ERR)from Drosophila melanogaster, Culex pipierm quinquefasciatus, Aedes aegypti, Nasonia vitripennis and Apis mellifera which were registered in Genbank, were analyzed and predicted by the tools of bioinformatics in the following aspects: the composition of nuclei acid sequences and amino acid sequences, protein physical and chemical properties, hydrophobicity or hydrophilicity, secondary and tertiary structures of protein, molecular phylogenetic evolution and so on. The results are as follows: ERR is a hydrophilic protein; the main motif of predicted secondary structure of ERR are alpha helix and random coil, beta turn and extended strand are spread in the whole secondary structure of protein;there are three β-strands and three α-helixs in DNA binding domain (DBD), and three β - strands and eleven α-helixs in ligand binding domain (LBD). The DBD is characterised by two Zinc-finger structures.