1eed | pdb_00001eed

X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors

spinqualitylabelsall models 1eed, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1eed is a 1 chain structure with sequence from Cryphonectria parasitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 0EO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP_CRYPA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structures of endothiapepsin, a fungal aspartic proteinase (EC 3.4.23.6), cocrystallized with two oligopeptide renin inhibitors, PD125967 and PD125754, have been determined at 2.0-A resolution and refined to R-factors of 0.143 and 0.153, respectively. These inhibitors, which are of the hydroxyethylene and statine types, respectively, possess a cyclohexylalanine side chain at P1 and have interesting functionalities at the P3 position which, until now, have not been subjected to crystallographic analysis. PD125967 has a bis(1-naphthylmethyl)acetyl residue at P3, and PD125754 possesses a hydroxyethylene analogue of the P3-P2 peptide bond for proteolytic stability. The structures reveal that the S3 pocket accommodates one naphthyl ring with conformational changes of the Asp 77 and Asp 114 side chains, the other naphthyl group residing in the S4 region. The P3-P2 hydroxyethylene analogue of PD125754 forms a hydrogen bond with the NH of Thr 219, thereby making the same interaction with the enzyme as the equivalent peptide groups of all inhibitors studied so far. The absence of side chains at the P2 and P1' positions of this inhibitor allows water molecules to occupy the respective pockets in the complex. The relative potencies of PD125967 and PD125754 for endothiapepsin are consistent with the changes in solvent-accessible area which take place on inhibitor binding. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.,Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM Biochemistry. 1992 Sep 8;31(35):8142-50. PMID:1525155 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

Proteopedia Page Contributors and Editors (what is this?)

OCA