Team:Stockholm/Project Idea/Proteins

Proteins

Superoxide dismutase 1 (SOD1)

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 Escherichia coli by Hallewell et al., (1985).

Gene (cDNA)		3D structure of human SOD1 in its dimeric form. Primary citation Leinartaite et al. (2010)
Length	465 bp
Edited nucleotide(s)	nt331 A → G
Removed restr. site(s)	PfeI
GenBank	AY450286.1
Protein
Length	154 aa
Size	15,936 Da
Fasta	SOD1
First reported by Hallewell et al., (1985).

Yeast copper chaperon (yCCS)

Yeast copper chaperon protein (yCCS) is a helper 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.

Gene (cDNA)		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
Length	750 bp
Edited nucleotide(s)	nt257 T → C
Removed restr. site(s)	EcoRI
GenBank	NM_001182535.1
Protein
Length	249 aa
Size	27,330 Da
Fasta	yCCS
First reported by Culotta et al. (1997).

Human basic fibroblast growth factor (bFGF)

Gene (cDNA)		3D structure of bFGF. Primary citation Bae et al. 2010
Length	468 bp
Edited nucleotide(s)	nt341 C → T
Removed restr. site(s)	AgeI
GenBank
Protein
Length	155 aa
Size	17,353 Da
Fasta	bFGF
First reported by <unknown>

Protein A, z domain

Part:BBa_K380009

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GenBank:

First reported by:

IgG protease, IdeS

Part:BBa_K380010

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

GenBank:

First reported by: