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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/44267

Title: In silico prediction and in vitro characterization of unique function of human RNase3
Authors: Pei-Chun Lien
Chien-Jung Chen
Ping-Hsueh Kuo
Tun-Wen Pai
Hsiu-Hui Chang
Yiu-Kay Lai
Wei-Shuo Wu
Margaret Dah-Tsyr Chang
Contributors: 國立臺灣海洋大學:資訊工程學系
NTOU:Department of Computer Science and Engineering
Keywords: Proteins
Neodymium
Peptides
Humans
Lipidomics
Amino acids
Biomembranes
Date: 2012-07
Issue Date: 2017-11-20T08:36:34Z
Publisher: The 6th International Conference on Complex, Intelligent, and Software Intensive Systems (CISIS 2012)
Abstract: Abstract:Ribonucleases (RNases) constitute a cellular function of exo- and endo-nucleases in all living organisms include vertebrate, bacteria, mold and plant. Human ribonuclease A (hRNaseA) super family consists of thirteen members with high structure similarities. Among which hRNase3 has multiple functions such as RNase, cytotoxicity, and heap ran sulfate (HS) binding activity. Employing Clustal W2 multiple sequence alignment of 13 human RNase A family members revealed that hRNase3 shares 67% identity and 76% similarity with hRNase2, much higher than the others. Besides, both RNase 2 and RNase3 are high conserved among primates. In terms of hRNase3-heparin/heparan sulfate (HS) interaction, three putative heparin binding regions (HBRs), 34RWRCK38 (HBR1), 75RSRFR79 (HBR2) and 101RPGRR105 (HBR3) have been predicted due to presence of positive charge clusters. Furthermore, these regions are also characterized as unique peptide regions within all 13 RNase sequences by REMUS system. Our experimental data derived from protein engineering and binding assays have demonstrated that these HBRs indeed involve in characteristic functions of hRNase3. In summary, through evolution hRNaseA super family has gained novel functions which may be preserved in the unique region or domain to account for additional molecular interactions.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/44267
Appears in Collections:[資訊工程學系] 演講及研討會

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