1hrn: Difference between revisions
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|PDB= 1hrn |SIZE=350|CAPTION= <scene name='initialview01'>1hrn</scene>, resolution 1.8Å | |PDB= 1hrn |SIZE=350|CAPTION= <scene name='initialview01'>1hrn</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CHA:1-HYDROXY-2-AMINO-3-CYCLOHEXYLPROPANE'>CHA</scene>, <scene name='pdbligand=CPP:2-CYCLOPROPYLMETHYLENEPROPANAL'>CPP</scene>, <scene name='pdbligand=IP3:1-HYDROXY-3-METHYLBUTANE'>IP3</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PPP:3-PHENYL-1,2-PROPANDIOL'>PPP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrn OCA], [http://www.ebi.ac.uk/pdbsum/1hrn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hrn RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The crystal structures of recombinant glycosylated human renin in complex with several polyhydroxymonoamide inhibitors have been determined at up to 1.8 A resolution. The high resolution structures permit a detailed analysis of the conformation of renin, the interactions between the inhibitors and renin, and the network of ordered water molecules. The polyhydroxymonoamide inhibitors are bound with their backbones in an extended conformation, and with their side-chains occupying the S3 to S1 pockets. The inhibited renin molecules are shown to exist in both the closed and the open conformations. Inhibitors bound to the two distinct forms of renin can assume different conformations at the P3 position. | The crystal structures of recombinant glycosylated human renin in complex with several polyhydroxymonoamide inhibitors have been determined at up to 1.8 A resolution. The high resolution structures permit a detailed analysis of the conformation of renin, the interactions between the inhibitors and renin, and the network of ordered water molecules. The polyhydroxymonoamide inhibitors are bound with their backbones in an extended conformation, and with their side-chains occupying the S3 to S1 pockets. The inhibited renin molecules are shown to exist in both the closed and the open conformations. Inhibitors bound to the two distinct forms of renin can assume different conformations at the P3 position. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Anderson, P C.]] | [[Category: Anderson, P C.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
[[Category: aspartic proteinase]] | [[Category: aspartic proteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:31 2008'' | ||
