This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3nod

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3nod.gif|left|200px]]
+
{{Seed}}
 +
[[Image:3nod.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3nod| PDB=3nod | SCENE= }}
{{STRUCTURE_3nod| PDB=3nod | SCENE= }}
-
'''MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE'''
+
===MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE===
-
==Overview==
+
<!--
-
Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitric oxide. Pterin binding refolds the central interface region, recruits new structural elements, creates a 30 angstrom deep active-center channel, and causes a 35 degrees helical tilt to expose a heme edge and the adjacent residue tryptophan-366 for likely reductase domain interactions and caveolin inhibition. Heme propionate interactions with pterin and L-Arg suggest that pterin has electronic influences on heme-bound oxygen. L-Arginine binds to glutamic acid-371 and stacks with heme in an otherwise hydrophobic pocket to aid activation of heme-bound oxygen by direct proton donation and thereby differentiate the two chemical steps of nitric oxide synthesis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9516116}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9516116 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9516116}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Thiocitrulline no]]
[[Category: Thiocitrulline no]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:08:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:57:40 2008''

Revision as of 09:57, 3 July 2008

Image:3nod.png

Template:STRUCTURE 3nod

MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE

Template:ABSTRACT PUBMED 9516116

About this Structure

3NOD is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of nitric oxide synthase oxygenase dimer with pterin and substrate., Crane BR, Arvai AS, Ghosh DK, Wu C, Getzoff ED, Stuehr DJ, Tainer JA, Science. 1998 Mar 27;279(5359):2121-6. PMID:9516116

Page seeded by OCA on Thu Jul 3 12:57:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nod"
Personal tools