2bpx: Difference between revisions

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==Overview==

The ability to replace an inhibitor bound to the HIV-1 protease in single, crystals with other potent inhibitors offers the possibility of, investigating a series of protease inhibitors rapidly and conveniently, with the use of X-ray crystallography. This approach affords a fast, turnaround of structural information for iterative rational drug designs, and obviates the need for studying the complex structures by, co-crystallization. The replacement approach has been successfully used, with single crystals of the HIV-1 protease complexed with a weak, inhibitor. The structures of the complexes obtained by the replacement, method are similar to those determined by co-crystallization.

The ability to replace an inhibitor bound to the HIV-1 protease in single crystals with other potent inhibitors offers the possibility of investigating a series of protease inhibitors rapidly and conveniently with the use of X-ray crystallography. This approach affords a fast turnaround of structural information for iterative rational drug designs and obviates the need for studying the complex structures by co-crystallization. The replacement approach has been successfully used with single crystals of the HIV-1 protease complexed with a weak inhibitor. The structures of the complexes obtained by the replacement method are similar to those determined by co-crystallization.

==About this Structure==

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[[Category: hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 17~~:16:33 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:20 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The ability to replace an inhibitor bound to the HIV-1 protease in single, crystals with other potent inhibitors offers the possibility of, investigating a series of protease inhibitors rapidly and conveniently, with the use of X-ray crystallography. This approach affords a fast, turnaround of structural information for iterative rational drug designs, and obviates the need for studying the complex structures by, co-crystallization. The replacement approach has been successfully used, with single crystals of the HIV-1 protease complexed with a weak, inhibitor. The structures of the complexes obtained by the replacement, method are similar to those determined by co-crystallization.
+The ability to replace an inhibitor bound to the HIV-1 protease in single crystals with other potent inhibitors offers the possibility of investigating a series of protease inhibitors rapidly and conveniently with the use of X-ray crystallography. This approach affords a fast turnaround of structural information for iterative rational drug designs and obviates the need for studying the complex structures by co-crystallization. The replacement approach has been successfully used with single crystals of the HIV-1 protease complexed with a weak inhibitor. The structures of the complexes obtained by the replacement method are similar to those determined by co-crystallization.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:16:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:20 2008''