2er6

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[[Image:2er6.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_2er6| PDB=2er6 | SCENE= }}
{{STRUCTURE_2er6| PDB=2er6 | SCENE= }}
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'''THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.'''
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===THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.===
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==Overview==
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The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X-ray diffraction at 0.20-nm resolution and refined to an agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu (R = -CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side-chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.
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The line below this paragraph, {{ABSTRACT_PUBMED_3119339}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 3119339 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3119339}}
==About this Structure==
==About this Structure==
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[[Category: Foundling, S I.]]
[[Category: Foundling, S I.]]
[[Category: Szelke, M.]]
[[Category: Szelke, M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:01:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:35:41 2008''

Revision as of 03:35, 29 July 2008

Template:STRUCTURE 2er6

THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.

Template:ABSTRACT PUBMED 3119339

About this Structure

2ER6 is a Single protein structure of sequence from Cryphonectria parasitica. Full crystallographic information is available from OCA.

Reference

The structure of a synthetic pepsin inhibitor complexed with endothiapepsin., Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M, Eur J Biochem. 1987 Nov 16;169(1):215-21. PMID:3119339

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