Nature. 1992 Jun 11;357(6378):466-72.

X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.

Dhanaraj V, Dealwis CG, Frazao C, Badasso M, Sibanda BL, Tickle IJ, Cooper JB, Driessen HP, Newman M, Aguilar C, et al.

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Department of Crystallography, Birkbeck College, London, UK.

Abstract

X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates.

PMID:: 1608447; [PubMed - indexed for MEDLINE]

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X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen. [J Mol Biol. 1994]
X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen.
Dealwis CG, Frazao C, Badasso M, Cooper JB, Tickle IJ, Driessen H, Blundell TL, Murakami K, Miyazaki H, Sueiras-Diaz J. J Mol Biol. 1994 Feb 11; 236(1):342-60.
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Cited by 6 PubMed Central articles

Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes. [Protein Sci. 2001]
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Andreeva NS, Rumsh LD. Protein Sci. 2001 Dec; 10(12):2439-50.
Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. [EMBO J. 1993]
Two crystal structures for cathepsin D: the lysosomal targeting signal and active site.
Metcalf P, Fusek M. EMBO J. 1993 Apr; 12(4):1293-302.
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin. [Biochem J. 1993]
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
Bailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M. Biochem J. 1993 Jan 15; 289 ( Pt 2):363-71.

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Structures reported by this article

The 3-D Structure Of Mouse Submaxillary Renin Complexed With A Decapeptide Inhibitor Ch-66 Based On The 4-16 Fragment Of Rat Angiotensinogen

PDB: 1SMR

Source: Mus musculus, synthetic construct

Method: X-Ray Diffraction

Resolution: 2 Å

See all 2 structures...

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X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.

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