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2er7

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[[Image:2er7.gif|left|200px]]
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{{STRUCTURE_2er7| PDB=2er7 | SCENE= }}
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'''X-RAY ANALYSES OF ASPARTIC PROTEINASES.III. THREE-DIMENSIONAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH A TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN AT 1.6 ANGSTROMS RESOLUTION'''
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===X-RAY ANALYSES OF ASPARTIC PROTEINASES.III. THREE-DIMENSIONAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH A TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN AT 1.6 ANGSTROMS RESOLUTION===
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==Overview==
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The aspartic proteinase, endothiapepsin (EC 3.4.23.6), was complexed with a highly potent renin inhibitor, H-261 (t-Boc-His-Pro-Phe-His-LeuOHVal-Ile-His), where OH denotes a hydroxyethylene (-(S) CHOH-CH2-) transition-state isostere in the scissile bond surrogate. Crystals were grown in a form that has the same space group P2(1) as the uncomplexed enzyme, but with a 10 A decrease in the length of the alpha-axis and a 13 degrees decrease in the beta-angle. X-ray data have been collected to a resolution of 1.6 A. The rotation and translation parameters defining the position of the enzyme in the unit cell were determined previously using another enzyme-inhibitor complex that crystallized isomorphously with that of H-261. The molecule was refined using restrained least-squares refinement and the positions of non-hydrogen atoms of the inhibitor and water molecules were defined by difference Fourier techniques. The enzyme-inhibitor complex and 322 water molecules were further refined to a crystallographic R-factor of 0.14. Apart from a small rigid group rotation of a domain comprising residues 190 to 302 and small movements in the flap, there is little difference in conformation between the complexed and uncomplexed forms of the enzyme. The inhibitor is bound in an extended conformation along the active site cleft, and the hydroxyl group of the hydroxyethylene moiety is hydrogen-bonded to both catalytic aspartate carboxylates. The complex is stabilized by hydrogen bonds between the main-chain of the inhibitor and the enzyme. All side-chains of the inhibitor are in van der Waals' contact with groups in the enzyme and define a series of specificity pockets along the active site cleft. The study provides useful clues as to how this potent renin inhibitor (IC50 value of 0.7 x 10(-9) M) may bind renin. In particular it defines the interactions of the hydroxyethylene transition-state isostere with the enzyme more precisely than has been previously possible and therefore provides a useful insight into interactions in the transition state complex.
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(as it appears on PubMed at http://www.pubmed.gov), where 2266553 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2266553}}
==About this Structure==
==About this Structure==
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[[Category: Szelke, M.]]
[[Category: Szelke, M.]]
[[Category: Veerapandian, B.]]
[[Category: Veerapandian, B.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:01:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:26:21 2008''

Revision as of 14:26, 28 July 2008

Image:2er7.png

Template:STRUCTURE 2er7

X-RAY ANALYSES OF ASPARTIC PROTEINASES.III. THREE-DIMENSIONAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH A TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN AT 1.6 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2266553

About this Structure

2ER7 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution., Veerapandian B, Cooper JB, Sali A, Blundell TL, J Mol Biol. 1990 Dec 20;216(4):1017-29. PMID:2266553

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