1995 Fiscal Year Final Research Report Summary
Classification of Protein Modules
| Project/Area Number |
06454664
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Nagoya University |
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Principal Investigator |
GO Mitiko Nagoya University, Biology, Professor, 理学部, 教授 (70037290)
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| Co-Investigator(Kenkyū-buntansha) |
YURA Kei Nagoya University, Biology, Researcher Associate, 理学部, 助手 (50252226)
NOGUTI Tosiyuki Nagoya University, Biology, Associate Professor, 理学部, 助教授 (90172775)
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| Project Period (FY) |
1994 – 1995
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| Keywords | module / intron / exon shuffling / protein tertiary structure / functional unit / molecular dynamics / molecular evolution / helix-turn-helix |
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| Research Abstract |
Introns are located close to boundaries of modules, small structural units in globular proteins. This fact implies that modules are the original building blocks encoded by exons and they were fused or shuffled during molecular evolution. The purpose of this research project is to classify the modules of proteins and to indentify the common modules recruited into different proteins by fusion or shuffling.
1.Development of classification method : We found by molecular dynamics calculation that the modules were able to be classified into groups on the basis of the similarity in their three-dimensional (3D) structures.
2.Classification of modules : Seventy-seven proteins with sequence identity less than 40% among one another were decomposed into 950 modules. About 2/3 of them were classified into 66 groups, however, the other modules were remained without making groups together.
3.Common modules observed in proteins : These modules had common biological functions. this result gives good evidence for exon/module shuffling among different proteins. The helix-turn-helix module seems to have diverged into three types with different roles ; the first is specific DNA sequence recognition, the second is non-specific DNA binding through the interactions with phosphates, and the third is scaffold stabilizing globular proteins.
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