Structural analysis of SNARE motifs from sea perch, Lateolabrax japonicus by computerized approaches | |
Chen, Kui; Huang, Xiaohang | |
刊名 | COMPUTATIONAL BIOLOGY AND CHEMISTRY
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2007-10-01 | |
卷号 | 31期号:5-6页码:378-383 |
关键词 | Sea Perch Snare Proteins Motif 7s Core Complex Protein Structure Analysis |
ISSN号 | 1476-9271 |
DOI | 10.1016/j.compbiolchem.2007.08-002 |
文献子类 | Article |
英文摘要 | Three cDNA sequences encoding four SNARE (N-ethylmaleimide-sensitive fusion protein attachment protein receptors) motifs were cloned from sea perch, and the deduced peptide sequences were analyzed for structural prediction by using 14 different web servers and softwares. The "ionic layer" structure, the three dimensional extension and conformational characters of the SNARE 7S core complex by using bioinformatics approaches were compared respectively with those from mammalian X-ray crystallographic investigations. The result suggested that the formation and stabilization of fish SNARE core complex might be driven by hydrophobic association, hydrogen bond among R group of core amino acids and electrostatic attraction at molecular level. This revealed that the SNARE proteins interaction of the fish may share the same molecular mechanism with that of mammal, indicating the universality and solidity of SNARE core complex theory. This work is also an attempt to get the protein 3D structural information which appears to be similar to that obtained through X-ray crystallography, only by using computerized approaches. (C) 2007 Elsevier Ltd. All rights reserved.; Three cDNA sequences encoding four SNARE (N-ethylmaleimide-sensitive fusion protein attachment protein receptors) motifs were cloned from sea perch, and the deduced peptide sequences were analyzed for structural prediction by using 14 different web servers and softwares. The "ionic layer" structure, the three dimensional extension and conformational characters of the SNARE 7S core complex by using bioinformatics approaches were compared respectively with those from mammalian X-ray crystallographic investigations. The result suggested that the formation and stabilization of fish SNARE core complex might be driven by hydrophobic association, hydrogen bond among R group of core amino acids and electrostatic attraction at molecular level. This revealed that the SNARE proteins interaction of the fish may share the same molecular mechanism with that of mammal, indicating the universality and solidity of SNARE core complex theory. This work is also an attempt to get the protein 3D structural information which appears to be similar to that obtained through X-ray crystallography, only by using computerized approaches. (C) 2007 Elsevier Ltd. All rights reserved. |
学科主题 | Biology ; Computer Science, Interdisciplinary Applications |
URL标识 | 查看原文 |
语种 | 英语 |
WOS记录号 | WOS:000250912400009 |
公开日期 | 2010-12-24 |
内容类型 | 期刊论文 |
源URL | [http://ir.qdio.ac.cn/handle/337002/5521] ![]() |
专题 | 海洋研究所_实验海洋生物学重点实验室 |
作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.State Ocean Adm, Inst Oceanog 1, Qingdao 266061, Peoples R China 3.Grad Univ Chinese Acad Sci, Beijing 100039, Peoples R China |
推荐引用方式 GB/T 7714 | Chen, Kui,Huang, Xiaohang. Structural analysis of SNARE motifs from sea perch, Lateolabrax japonicus by computerized approaches[J]. COMPUTATIONAL BIOLOGY AND CHEMISTRY,2007,31(5-6):378-383. |
APA | Chen, Kui,&Huang, Xiaohang.(2007).Structural analysis of SNARE motifs from sea perch, Lateolabrax japonicus by computerized approaches.COMPUTATIONAL BIOLOGY AND CHEMISTRY,31(5-6),378-383. |
MLA | Chen, Kui,et al."Structural analysis of SNARE motifs from sea perch, Lateolabrax japonicus by computerized approaches".COMPUTATIONAL BIOLOGY AND CHEMISTRY 31.5-6(2007):378-383. |
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