This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1d8v
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | We present the solution structure of MAP30, a plant protein with anti-HIV | + | 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== | ==About this Structure== | ||
| Line 16: | Line 16: | ||
[[Category: Neamati, N.]] | [[Category: Neamati, N.]] | ||
[[Category: Palmer, I.]] | [[Category: Palmer, I.]] | ||
| - | [[Category: Stahl, S | + | [[Category: Stahl, S J.]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, Y X.]] |
[[Category: single chain]] | [[Category: single chain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:10 2008'' |
Revision as of 10:14, 21 February 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 Thu Feb 21 12:14:10 2008
