2REN

STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION

Summary for 2REN

• Entry DOI: 10.2210/pdb2ren/pdb
• Descriptor: RENIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: hydrolase(acid proteinase)
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00797
• Total number of polymer chains: 1
• Total formula weight: 37488.22

Authors

Sielecki, A.R.,James, M.N.G. (deposition date: 1992-02-05, release date: 1994-01-31, Last modification date: 2024-11-06)

Primary citation

Sielecki, A.R.,Hayakawa, K.,Fujinaga, M.,Murphy, M.E.,Fraser, M.,Muir, A.K.,Carilli, C.T.,Lewicki, J.A.,Baxter, J.D.,James, M.N.
Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution.
Science, 243:1346-1351, 1989

PubMed Abstract: The x-ray crystal structure of recombinant human renin has been determined. Molecular dynamics techniques that included crystallographic data as a restraint were used to improve an initial model based on porcine pepsinogen. The present agreement factor for data from 8.0 to 2.5 angstroms (A) is 0.236. Some of the surface loops are poorly determined, and these disordered regions border a 30 A wide solvent channel. Comparison of renin with other aspartyl proteinases shows that, although the structural cores and active sites are highly conserved, surface residues, some of which are critical for specificity, vary greatly (up to 10A). Knowledge of the actual structure, as opposed to the use of models based on related enzymes, should facilitate the design of renin inhibitors.

PubMed: 2493678

Experimental method

X-RAY DIFFRACTION (2.5 Å)