2001 Fiscal Year Final Research Report Summary
The reaction mechanism of the ribonuclease T2 family
| Project/Area Number |
10672025
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Showa University |
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Principal Investigator |
NAKAMURA Kazuo Showa University, School of Pharmaceutical Sciences, Professor, 薬学部, 教授 (00012675)
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| Project Period (FY) |
1998 – 2001
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| Keywords | ribonuclease / X-ray structure determination / substrate analogue / subsite |
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| Research Abstract |
The RNase T2 family shows broad base specificity. The objects of the project on the RNase T2 family are to gain the base-recognition and catalytic mechanism of the RNase T2 family enzymes. The substrate-fragment complexs of RNase LE reveal interesting features : the substrate fragments (3'-GMP and 5'-GMP) and substrate analogue d(GpG) bound in the productive binding mode while inhibitor (2'-GMP) bound in the non-productive binding mode ; and the binding mode of 3'-GMP at the Bi subsite and that of 5'-GMP at the B2 site are similar to that of d(GpG) bound at both B 1 and B2 subsite. These observations show that the binding of substrate fragments may conform to the principles of additivity.
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