Team:Stockholm/Project Idea/Proteins

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Contents

Proteins

Superoxide dismutase 1 protein, SOD

Part:BBa_K380007


Human soluble superoxide dismutase 1 (SOD1) is a soluble cytoplasmic protein functional as a homodimer that binds copper and zink ions. SOD1 catalyzes the reaction O-2 + O-2 + 2H+ → H2O2 + O2, protecting the cell from oxidative damage. SOD1 was first cloned and expressed in E. coli by Hallewell et al., (1985).

3D structure of human SOD1 in it's dimeric form. Primary citation Leinartaite et al. (2010)
Gene (cDNA)
length 465 bp
removed restriction site PfeI
exchanged nt nt331 A → G
Protein
length 154 aa
size 15,936 Da
Fasta SOD1


GenBank:AY450286.1

First reported by:Hallewell et al., (1985).




copper chaperon protein for SOD, yCCS

Part:BBa_K380008


Yeast copper chaperon protein (yCCS) is a help chaperon specific for copper/zinc superoxide dismutase located to the cytoplasm. yCCS generates fully metallized, active SOD1 proteins that in turn protects the cell from oxidative damage.

yCCS has been shown to successfully mediate the delivery of copper ions to human SOD1 (Ahl et al. 2003). Co-expression of SOD1 and yCCS yields proteins with higher copper contents, leading to increased activity and more stable proteins.

3D structure of yCCS interacting with yeast superoxide dismutase (ySOD) in it's monomeric form. Ions indicated as gray orbs. Primary citation [Lamb et al. 2001]


Gene (cDNA)
length 750bp
removed restriction site EcoRI
exchanged nt nt257 T → C
Protein
length 249 aa
size 27,330 Da
Fasta yCCS


GenBank:NM_001182535.1

First reported by:Culotta et al. (1997).






Human basic fibroblast growth factor, bFGF

Part:BBa_K380006


3D structure of bFGF. Primary citation Bae et al. 2010


Gene (cDNA)
length 468 bp
removed restriction sites AgeI
exchanged nt 341 C → T
Protein
length 155 aa
size 17,353 Da
Fasta bFGF


GenBank:

First reported by:





Protein A, z domain

Part:BBa_K380009


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Genepart
length 174 bp
removed restriction sites -
exchanged nt -
Protein
length 58 aa
size
Fasta


GenBank:

First reported by:






IgG protease, IdeS

Part:BBa_K380010


3D structure of IdeS. Primary citation Wenig et al. 2004


Gene (cDNA)
length 930 bp
removed restriction sites -
exchanged nt -
Protein
length 339 aa
size 37,977 Da
Fasta IdeS


GenBank:

First reported by:







The Faculty of Science at Stockholm University Swedish Vitiligo association (Svenska Vitiligoförbundet) Geneious Fermentas/ Sigma-Aldrich/