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1d8v
From Proteopedia
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'''THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.''' | '''THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.''' | ||
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[[Category: Stahl, S J.]] | [[Category: Stahl, S J.]] | ||
[[Category: Wang, Y X.]] | [[Category: Wang, Y X.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:34:47 2008'' | |
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Revision as of 10:34, 2 May 2008
THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.
Overview
We present the solution structure of MAP30, a plant protein with anti-HIV and anti-tumor activities. Structural analysis and subsequent biochemical assays lead to several novel discoveries. First, MAP30 acts like a DNA glycosylase/apurinic (ap) lyase, an additional activity distinct from its known RNA N-glycosidase activity toward the 28S rRNA. Glycosylase/ap lyase activity explains MAP30's apparent inhibition of the HIV-1 integrase, MAP30's ability to irreversibly relax supercoiled DNA, and may be an alternative cytotoxic pathway that contributes to MAP30's anti-HIV/anti-tumor activities. Second, two distinct, but contiguous, subsites are responsible for MAP30's glycosylase/ap lyase activity. Third, Mn2+ and Zn2+ interact with negatively charged surfaces next to the catalytic sites, facilitating DNA substrate binding instead of directly participating in catalysis.
About this Structure
1D8V is a Single protein structure of sequence from Momordica charantia. Full crystallographic information is available from OCA.
Reference
Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions., Wang YX, Neamati N, Jacob J, Palmer I, Stahl SJ, Kaufman JD, Huang PL, Huang PL, Winslow HE, Pommier Y, Wingfield PT, Lee-Huang S, Bax A, Torchia DA, Cell. 1999 Nov 12;99(4):433-42. PMID:10571185 Page seeded by OCA on Fri May 2 13:34:47 2008
