2ntn: Difference between revisions

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==Overview==

The MabA protein from Mycobacterium tuberculosis is a validated drug, target. Previous structural studies of this protein showed dynamic, behaviour in the catalytic site and described motion between an open~~, ;~~active' holo form (with NADP) and a closed ;inactive' apo form (without, NADP). Here, a mutation (G139A) is reported that leads to complete protein, inactivation and freezes the catalytic site into its closed form, even in, the presence of the cofactor. This observation suggests a new way to, develop anti-MabA drugs via protein stabilization of the ;inactive' form.

The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open 'active' holo form (with NADP) and a closed 'inactive' apo form (without NADP). Here, a mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed form, even in the presence of the cofactor. This observation suggests a new way to develop anti-MabA drugs via protein stabilization of the 'inactive' form.

==About this Structure==

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[[Category: sdr]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 14~~:07:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:51 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The MabA protein from Mycobacterium tuberculosis is a validated drug, target. Previous structural studies of this protein showed dynamic, behaviour in the catalytic site and described motion between an open, ;active' holo form (with NADP) and a closed ;inactive' apo form (without, NADP). Here, a mutation (G139A) is reported that leads to complete protein, inactivation and freezes the catalytic site into its closed form, even in, the presence of the cofactor. This observation suggests a new way to, develop anti-MabA drugs via protein stabilization of the ;inactive' form.
+The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open 'active' holo form (with NADP) and a closed 'inactive' apo form (without NADP). Here, a mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed form, even in the presence of the cofactor. This observation suggests a new way to develop anti-MabA drugs via protein stabilization of the 'inactive' form.
 ==About this Structure==
@@ Line 24: / Line 24: @@
 [[Category: sdr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:07:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:51 2008''