1u8g: Difference between revisions

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==Overview==

Depending on the excess of ligand used for complex formation, the HIV-1, protease complexed with a novel phenylnorstatine inhibitor forms crystals, of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The, orthorhombic form shows an unusual complexity of crystal packing: in, addition to one inhibitor molecule that is bound to the enzyme active, site, the second inhibitor molecule is bound as an outer ligand at the, protein interface. Binding of the outer ligand apparently increases the, crystal-quality parameters so that the diffraction data allow solution of, the structure of the complex at 1.03 A, the best resolution reported to, date. The outer ligand interacts with all four surrounding HIV-1 protease, molecules and has a bent conformation owing to its accommodation in the, intermolecular space. The parameters of the solved structures of the, orthorhombic and hexagonal forms are compared.

Depending on the excess of ligand used for complex formation, the HIV-1 protease complexed with a novel phenylnorstatine inhibitor forms crystals of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The orthorhombic form shows an unusual complexity of crystal packing: in addition to one inhibitor molecule that is bound to the enzyme active site, the second inhibitor molecule is bound as an outer ligand at the protein interface. Binding of the outer ligand apparently increases the crystal-quality parameters so that the diffraction data allow solution of the structure of the complex at 1.03 A, the best resolution reported to date. The outer ligand interacts with all four surrounding HIV-1 protease molecules and has a bent conformation owing to its accommodation in the intermolecular space. The parameters of the solved structures of the orthorhombic and hexagonal forms are compared.

==About this Structure==

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[[Category: hydrolase/hydrolase inhibitor; aspartyl protease; human immunodeficiency virus; inhibitor design]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Depending on the excess of ligand used for complex formation, the HIV-1, protease complexed with a novel phenylnorstatine inhibitor forms crystals, of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The, orthorhombic form shows an unusual complexity of crystal packing: in, addition to one inhibitor molecule that is bound to the enzyme active, site, the second inhibitor molecule is bound as an outer ligand at the, protein interface. Binding of the outer ligand apparently increases the, crystal-quality parameters so that the diffraction data allow solution of, the structure of the complex at 1.03 A, the best resolution reported to, date. The outer ligand interacts with all four surrounding HIV-1 protease, molecules and has a bent conformation owing to its accommodation in the, intermolecular space. The parameters of the solved structures of the, orthorhombic and hexagonal forms are compared.
+Depending on the excess of ligand used for complex formation, the HIV-1 protease complexed with a novel phenylnorstatine inhibitor forms crystals of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The orthorhombic form shows an unusual complexity of crystal packing: in addition to one inhibitor molecule that is bound to the enzyme active site, the second inhibitor molecule is bound as an outer ligand at the protein interface. Binding of the outer ligand apparently increases the crystal-quality parameters so that the diffraction data allow solution of the structure of the complex at 1.03 A, the best resolution reported to date. The outer ligand interacts with all four surrounding HIV-1 protease molecules and has a bent conformation owing to its accommodation in the intermolecular space. The parameters of the solved structures of the orthorhombic and hexagonal forms are compared.
 ==About this Structure==
@@ Line 26: / Line 26: @@
 [[Category: hydrolase/hydrolase inhibitor; aspartyl protease; human immunodeficiency virus; inhibitor design]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:59:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:49 2008''