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

V. Dhanaraj; C. G. Dealwis; C. Frazao; M. Badasso; B. L. Sibanda; I. J. Tickle; J. B. Cooper; H. P. C. Driessen; M. Newman; C. Aguilar; S. P. Wood; T. L. Blundell; P. M. Hobart; K. F. Geoghegan; M. J. Ammirati; D. E. Danley; B. A. O'connor; D. J. Hoover

doi:10.1038/357466a0

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

V. Dhanaraj, C. G. Dealwis, C. Frazao, M. Badasso, B. L. Sibanda, I. J. Tickle, J. B. Cooper, H. P. C. Driessen, M. Newman, C. Aguilar, S. P. Wood, T. L. Blundell, P. M. Hobart, K. F. Geoghegan, M. J. Ammirati, D. E. Danley, B. A. O'connor, D. J. Hoover

Institute of Life Sciences and Healthcare

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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 Å, 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.

Original language	English
Pages (from-to)	466-472
Journal	Nature
Volume	357
Issue number	6378
DOIs	https://doi.org/10.1038/357466a0
Publication status	Published - 11 Jun 1992

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Dhanaraj, V., Dealwis, C. G., Frazao, C., Badasso, M., Sibanda, B. L., Tickle, I. J., Cooper, J. B., Driessen, H. P. C., Newman, M., Aguilar, C., Wood, S. P., Blundell, T. L., Hobart, P. M., Geoghegan, K. F., Ammirati, M. J., Danley, D. E., O'connor, B. A., & Hoover, D. J. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basisof specificity for human and mouse renins. Nature, 357(6378), 466-472. https://doi.org/10.1038/357466a0

@article{1de7a8ea724642c586e588b5f8062122,

title = "X-ray analyses of peptide–inhibitor complexes define the structural basisof specificity for human and mouse renins",

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 {\AA}, 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.",

author = "V. Dhanaraj and Dealwis, {C. G.} and C. Frazao and M. Badasso and Sibanda, {B. L.} and Tickle, {I. J.} and Cooper, {J. B.} and Driessen, {H. P. C.} and M. Newman and C. Aguilar and Wood, {S. P.} and Blundell, {T. L.} and Hobart, {P. M.} and Geoghegan, {K. F.} and Ammirati, {M. J.} and Danley, {D. E.} and O'connor, {B. A.} and Hoover, {D. J.}",

year = "1992",

month = jun,

day = "11",

doi = "10.1038/357466a0",

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volume = "357",

pages = "466--472",

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Dhanaraj, V, Dealwis, CG, Frazao, C, Badasso, M, Sibanda, BL, Tickle, IJ, Cooper, JB, Driessen, HPC, Newman, M, Aguilar, C, Wood, SP, Blundell, TL, Hobart, PM, Geoghegan, KF, Ammirati, MJ, Danley, DE, O'connor, BA & Hoover, DJ 1992, 'X-ray analyses of peptide–inhibitor complexes define the structural basisof specificity for human and mouse renins', Nature, vol. 357, no. 6378, pp. 466-472. https://doi.org/10.1038/357466a0

TY - JOUR

T1 - X-ray analyses of peptide–inhibitor complexes define the structural basisof specificity for human and mouse renins

AU - Dhanaraj, V.

AU - Dealwis, C. G.

AU - Frazao, C.

AU - Badasso, M.

AU - Sibanda, B. L.

AU - Tickle, I. J.

AU - Cooper, J. B.

AU - Driessen, H. P. C.

AU - Newman, M.

AU - Aguilar, C.

AU - Wood, S. P.

AU - Blundell, T. L.

AU - Hobart, P. M.

AU - Geoghegan, K. F.

AU - Ammirati, M. J.

AU - Danley, D. E.

AU - O'connor, B. A.

AU - Hoover, D. J.

PY - 1992/6/11

Y1 - 1992/6/11

N2 - 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 Å, 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.

AB - 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 Å, 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.

U2 - 10.1038/357466a0

DO - 10.1038/357466a0

M3 - Article

SN - 0028-0836

VL - 357

SP - 466

EP - 472

JO - Nature

JF - Nature

IS - 6378

ER -

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

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