1bil: Difference between revisions

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|PDB= 1bil |SIZE=350|CAPTION= <scene name='initialview01'>1bil</scene>, resolution 2.4&Aring;
|PDB= 1bil |SIZE=350|CAPTION= <scene name='initialview01'>1bil</scene>, resolution 2.4&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=DMF:DIMETHYLFORMAMIDE'>DMF</scene>, <scene name='pdbligand=PHC:N-METHYL-N-(METHYLBENZYL)FORMAMIDE'>PHC</scene>, <scene name='pdbligand=HII:2-METHYL-3-(2-AMINOTHIAZOLO)PROPANAL'>HII</scene> and <scene name='pdbligand=IP3:1-HYDROXY-3-METHYLBUTANE'>IP3</scene>
|LIGAND= <scene name='pdbligand=CHA:1-HYDROXY-2-AMINO-3-CYCLOHEXYLPROPANE'>CHA</scene>, <scene name='pdbligand=DMF:DIMETHYLFORMAMIDE'>DMF</scene>, <scene name='pdbligand=HII:2-METHYL-3-(2-AMINOTHIAZOLO)PROPANAL'>HII</scene>, <scene name='pdbligand=IP3:1-HYDROXY-3-METHYLBUTANE'>IP3</scene>, <scene name='pdbligand=PHC:N-METHYL-N-(METHYLBENZYL)FORMAMIDE'>PHC</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE= CMV IE-HUMAN PREPRORENIN CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= CMV IE-HUMAN PREPRORENIN CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bil OCA], [http://www.ebi.ac.uk/pdbsum/1bil PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bil RCSB]</span>
}}
}}


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==Overview==
==Overview==
The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
==Disease==
Known diseases associated with this structure: Hyperproreninemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=179820 179820]], Renal tubular dysgenesis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=179820 179820]]


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Tong, L.]]
[[Category: Tong, L.]]
[[Category: DMF]]
[[Category: HII]]
[[Category: IP3]]
[[Category: PHC]]
[[Category: aspartic proteinase]]
[[Category: aspartic proteinase]]


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