BAIT

NOS3

ECNOS, eNOS
nitric oxide synthase 3 (endothelial cell)
GO Process (26)
GO Function (11)
GO Component (7)
Homo sapiens
PREY

CALM1

CaMI, rCG_20808
calmodulin 1
GO Process (21)
GO Function (19)
GO Component (14)
Rattus norvegicus

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural basis for endothelial nitric oxide synthase binding to calmodulin.

Aoyagi M, Arvai AS, Tainer JA, Getzoff ED

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 ... [more]

EMBO J. Feb. 17, 2003; 22(4);766-75 [Pubmed: 12574113]

Throughput

  • Low Throughput

Additional Notes

  • CaM-binding region (residues 492 to 511) of NOS3 used for structure

Curated By

  • BioGRID