1niw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1niw.jpg|left|200px]]<br /><applet load="1niw" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1niw.jpg|left|200px]]
-
caption="1niw, resolution 2.05&Aring;" />
+
 
-
'''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin'''<br />
+
{{Structure
 +
|PDB= 1niw |SIZE=350|CAPTION= <scene name='initialview01'>1niw</scene>, resolution 2.05&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1NIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].
+
1NIW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA].
==Reference==
==Reference==
-
Structural basis for endothelial nitric oxide synthase binding to calmodulin., Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, EMBO J. 2003 Feb 17;22(4):766-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12574113 12574113]
+
Structural basis for endothelial nitric oxide synthase binding to calmodulin., Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, EMBO J. 2003 Feb 17;22(4):766-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12574113 12574113]
[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 26: Line 35:
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
[[Category: nitric oxide]]
[[Category: nitric oxide]]
-
[[Category: nos]]
+
[[Category: no]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:33 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:29 2008''

Revision as of 10:57, 20 March 2008


PDB ID 1niw

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands: , and
Activity: Nitric-oxide synthase, with EC number 1.14.13.39
Coordinates: save as pdb, mmCIF, xml



Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin


Contents

Overview

The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue peptide comprising the endothelial NOS (eNOS) CaM-binding region establishes their individual conformations and intermolecular interactions, and suggests the basis for isozyme-specific differences. The alpha-helical eNOS peptide binds in an antiparallel orientation to CaM through extensive hydrophobic interactions. Unique NOS interactions occur with: (i). the CaM flexible central linker, explaining its importance in NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific requirement for a bulky, hydrophobic residue at position 144. This binding mode expands mechanisms for CaM-mediated activation, explains eNOS deactivation by Thr495 phosphorylation, and implicates specific hydrophobic residues in the Ca(2+) independence of inducible NOS.

Disease

Known diseases associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[163729], Coronary spasms, susceptibility to OMIM:[163729], Hypertension, pregnancy-induced OMIM:[163729], Hypertension, susceptibility to OMIM:[163729], Ischemic stroke, susceptibility to OMIM:[163729], Placental abruption OMIM:[163729]

About this Structure

1NIW is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis for endothelial nitric oxide synthase binding to calmodulin., Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, EMBO J. 2003 Feb 17;22(4):766-75. PMID:12574113

Page seeded by OCA on Thu Mar 20 12:57:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools