1d1w: Difference between revisions

Revision as of 22:08, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1d1w.png

Template:STRUCTURE 1d1w

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)

Template:ABSTRACT PUBMED 11051558

About this StructureAbout this Structure

1D1W is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas., Li H, Raman CS, Martasek P, Kral V, Masters BS, Poulos TL, J Inorg Biochem. 2000 Aug 31;81(3):133-9. PMID:11051558

Page seeded by OCA on Mon Jun 30 22:08:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)'''
+===BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 2-AMINOTHIAZOLINE (H4B BOUND)===
-==Overview==
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-Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_11051558}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11051558 is the PubMed ID number.
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 [[Category: Raman, C S.]]
 [[Category: Alpha-beta fold]]
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