1bim
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1bim |SIZE=350|CAPTION= <scene name='initialview01'>1bim</scene>, resolution 2.8Å | |PDB= 1bim |SIZE=350|CAPTION= <scene name='initialview01'>1bim</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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=IP4:1-METHYL-2-OXY-5,5-DIMETHYL+PYRROLIDINE'>IP4</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=1bim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bim OCA], [http://www.ebi.ac.uk/pdbsum/1bim PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bim RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==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== | ||
| Line 26: | Line 26: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| - | [[Category: DMF]] | ||
| - | [[Category: HII]] | ||
| - | [[Category: IP4]] | ||
| - | [[Category: PHC]] | ||
[[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 19:01:44 2008'' |
Revision as of 16:01, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | CMV IE-HUMAN PREPRORENIN CDNA (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
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.
About this Structure
1BIM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors., Tong L, Pav S, Lamarre D, Simoneau B, Lavallee P, Jung G, J Biol Chem. 1995 Dec 8;270(49):29520-4. PMID:7493993
Page seeded by OCA on Sun Mar 30 19:01:44 2008
