1r1i

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{{STRUCTURE_1r1i| PDB=1r1i | SCENE= }}
{{STRUCTURE_1r1i| PDB=1r1i | SCENE= }}
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'''STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS'''
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===STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS===
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==Overview==
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Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor. Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents. Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described. The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 14747736 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14747736}}
==About this Structure==
==About this Structure==
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[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
[[Category: Lt1_9]]
[[Category: Lt1_9]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:57:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:34:43 2008''

Revision as of 01:34, 28 July 2008

Template:STRUCTURE 1r1i

STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS

Template:ABSTRACT PUBMED 14747736

About this Structure

1R1I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural analysis of neprilysin with various specific and potent inhibitors., Oefner C, Roques BP, Fournie-Zaluski MC, Dale GE, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):392-6. Epub 2004, Jan 23. PMID:14747736

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