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六品系猪SLA-2多肽结合区分子结构差异研究
引用本文:白婧,李云岗,张强,赵德,冯磊,高凤山.六品系猪SLA-2多肽结合区分子结构差异研究[J].宁夏大学学报(自然科学版),2012,33(3):274-278.
作者姓名:白婧  李云岗  张强  赵德  冯磊  高凤山
作者单位:1. 大连大学生命科学与技术学院,辽宁大连,116622
2. 山东省动物疾病预防与控制中心,山东济南,250022
3. 家畜疫病病原微生物国家重点实验室中国农业科学院兰州兽医研究所,甘肃兰州,730046
4. 大连大学生命科学与技术学院,辽宁大连 116622;山东省动物疾病预防与控制中心,山东济南250022
基金项目:国家自然科学基金资助项目(30972169,31172304);辽宁省教育厅科学计划基金资助项目(L2010018)
摘    要:为研究我国饲养的不同品系猪sLA_2抗原多肽结合区分子结构差异,设计引物,克隆了六品系猪SLA-2基因cDNA全长序列,用分子生物学软件分析其基因特征,比较各品系猪SLA-2分子结构差异,并通过同源模建显示变异住点的空间位置.结果表明,六品系猪SLA-2cDNA全长为1119bp,其中3-1097为编码区,共编码364个氨基酸,分别在第125,188,227,283位置出现半胱氨酸残基,含有2对链内二硫键.六品系猪SLA-2胞外区氨基酸差异主要集中在α1区的62-70及77-82和口2区的143-156.同源模建显示,这些变异位点均位于SLA-2多肽结合区的口螺旋结构上,推测可能与动物的抗病毒免疫特性有关.可为猪品系的改良及抗病毒免疫研究提供参考.

关 键 词:  多肽结合区  分子结构

Analyzing the Difference of Peptide-binding Domain in SLA-2 from Six Breeds of Pigs
Bai Jing , Li Yungang , Zhang Qiang , Zhao De , Feng Lei , Gao Fengshan.Analyzing the Difference of Peptide-binding Domain in SLA-2 from Six Breeds of Pigs[J].Journal of Ningxia University(Natural Science Edition),2012,33(3):274-278.
Authors:Bai Jing  Li Yungang  Zhang Qiang  Zhao De  Feng Lei  Gao Fengshan
Affiliation:1,2 (1.College of Life Science and Technology,Dalian University,Dalian 116622,China; 2.Shandong Center for Animal Disease Control and Prevention,Jinan 250022,China; 3.Veterinary Research Institute,Chinese Academy of Agricultural Sciences,Lanzou 730046,China)
Abstract:In order to study the molecular structure difference in peptide-binding domain(PBD)of SLA-2 from the main breeds of pigs raised in China,a pair of primers were designed to amplify the whole cDNA of SLA-2 from six breeds of pigs and then the genetic characteristics of the interest genes were analyzed by computer.The molecular structure difference in PBD of SLA-2 from six breeds of pigs were further analyzed followed by homology modeling to display the key variable amino acids.After cloning,sequencing and analyzing by computer,all SLA-2 alleles were 1 119bp and the 3-1 097 sites were the ORF domain which coded for 364 amino acids with two sets of disulfide bond in intro-chain constituted by four cysteines situated in 125,188,227 and 283 sites.The main variable amino acids of extra-cellular domain of SLA-2 in six breeds of pigs focused on 62-70 sites and 77-82 sites in α1 domain,and 143-156 sites in α2 domain.Homology modeling displayed that all variable amino acids located on the α-Helix strains PBD of SLA-2 molecule,which indicated that they might be associated with the anti-virus immune activity for these breeds of pigs.The study will supply significant data for improving the anti-virus capacity for the cultivated breed of swine.
Keywords:pig  peptide-binding domain  molecular structure
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