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| - | [[Image:1zdp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1zdp| PDB=1zdp | SCENE= }} | | {{STRUCTURE_1zdp| PDB=1zdp | SCENE= }} |
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| - | '''Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan'''
| + | ===Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan=== |
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| - | ==Overview==
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| - | The three-dimensional structures of (S)-thiorphan and (R)-retro-thiorphan bound to thermolysin have been determined crystallographically and refined to residuals of 0.183 and 0.187 at 1.7-A resolution. Thiorphan [N-[(S)-2-(mercaptomethyl)-1-oxo-3-phenylpropyl]glycine] [HSCH2CH(CH2C6H5)CONHC-H2COOH] and retro-thiorphan [[[(R)-1-(mercaptomethyl)-2-phenylethyl] amino]-3-oxopropanoic acid] [HSCH2CH(CH2C6H5)NHCOCH2COOH] are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase"). The mode of binding of thiorphan to thermolysin is similar to that of (2-benzyl-3-mercaptopropanoyl)-L-alanylglycinamide [Monzingo, A.F., & Matthews, B.W. (1982) Biochemistry 21, 3390-3394] with the inhibitor sulfur atom coordinated to the active site zinc and the peptide portion forming substrate-like interactions with the enzyme. The isomeric inhibitor retro-thiorphan, which differs from thiorphan by the inversion of an amide bond, utilizes very similar interactions with enzyme. Despite the inversion of the -CO-NH- linkage the carbonyl oxygen and amide nitrogen display very similar hydrogen bonding, as anticipated by B.P. Roques et al. [(1983) Proc. Natl. Acad. Sci. U.S.A. 80, 3178-3182]. These results explain why thermolysin and possibly other zinc endopeptidases such as endopeptidase EC 24-11 fail to discriminate between these retro-inverso inhibitors.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_2719912}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2719912 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_2719912}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Thermostable]] | | [[Category: Thermostable]] |
| | [[Category: Zinc endopeptidase]] | | [[Category: Zinc endopeptidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:30:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:00:52 2008'' |
Revision as of 03:00, 28 July 2008
Template:STRUCTURE 1zdp
Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan
Template:ABSTRACT PUBMED 2719912
About this Structure
1ZDP is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.
Reference
Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin., Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW, Biochemistry. 1989 Feb 21;28(4):1493-7. PMID:2719912
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