1t4o
From Proteopedia
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===Crystal structure of rnt1p dsRBD=== | ===Crystal structure of rnt1p dsRBD=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1t4o]] is a 2 chain structure of [[Ribonuclease]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4O OCA]. | |
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| + | ==See Also== | ||
| + | *[[Ribonuclease|Ribonuclease]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015192703</ref><references group="xtra"/> |
[[Category: Ribonuclease III]] | [[Category: Ribonuclease III]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Ares, M.]] | ||
[[Category: Edwards, T E.]] | [[Category: Edwards, T E.]] | ||
[[Category: Godin, K S.]] | [[Category: Godin, K S.]] | ||
[[Category: Graille, M.]] | [[Category: Graille, M.]] | ||
| - | [[Category: Jr., M Ares.]] | ||
[[Category: Leeper, T C.]] | [[Category: Leeper, T C.]] | ||
[[Category: Leulliot, N.]] | [[Category: Leulliot, N.]] | ||
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[[Category: Varani, G.]] | [[Category: Varani, G.]] | ||
[[Category: Dsrbd]] | [[Category: Dsrbd]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Rna-binding]] | [[Category: Rna-binding]] | ||
[[Category: Rnt1p]] | [[Category: Rnt1p]] | ||
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Revision as of 16:01, 26 July 2012
Contents |
Crystal structure of rnt1p dsRBD
Template:ABSTRACT PUBMED 15192703
About this Structure
1t4o is a 2 chain structure of Ribonuclease with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
See Also
Reference
- Leulliot N, Quevillon-Cheruel S, Graille M, van Tilbeurgh H, Leeper TC, Godin KS, Edwards TE, Sigurdsson ST, Rozenkrants N, Nagel RJ, Ares M, Varani G. A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III. EMBO J. 2004 Jul 7;23(13):2468-77. Epub 2004 Jun 10. PMID:15192703 doi:10.1038/sj.emboj.7600260
