1niw
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1niw.jpg|left|200px]] | [[Image:1niw.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1niw", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1niw| PDB=1niw | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin''' | '''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin''' | ||
Line 30: | Line 27: | ||
[[Category: Getzoff, E D.]] | [[Category: Getzoff, E D.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
- | [[Category: | + | [[Category: Calcium-binding protein]] |
- | [[Category: | + | [[Category: Nitric oxide]] |
- | [[Category: | + | [[Category: No]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:35:16 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 23:35, 2 May 2008
Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin
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.
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 Sat May 3 02:35:16 2008