Team:Stockholm/Project Idea/Proteins

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Contents

Proteins

Superoxide dismutase 1 protein, SOD

[http://partsregistry.org/Part:BBa_K380007 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 [http://www.ncbi.nlm.nih.gov/pubmed/3889846 Hallewell et al., (1985)].

3D structure of human SOD1 in it's dimeric form. Primary citation [http://www.ncbi.nlm.nih.gov/pubmed/20822138 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 [http://www.ncbi.nlm.nih.gov/protein/49456443?report=fasta SOD1]


GenBank:[http://www.ncbi.nlm.nih.gov/nucleotide/38489879?report=genbank&log$=nucltop&blast_rank=22&RID=CAM83NYN01S AY450286.1]

First reported by:[http://www.ncbi.nlm.nih.gov/pubmed/3889846 Hallewell et al., (1985)].




copper chaperon protein for SOD, yCCS

[http://partsregistry.org/Part:BBa_K380008 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 ([http://www.ncbi.nlm.nih.gov/pubmed/15358352 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 [[http://www.ncbi.nlm.nih.gov/pubmed/11524675 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 [http://www.ncbi.nlm.nih.gov/protein/596088?report=fasta yCCS]


GenBank:[http://www.ncbi.nlm.nih.gov/nuccore/NM_001182535.1?report=genbank&log$=seqview NM_001182535.1]

First reported by:[http://www.ncbi.nlm.nih.gov/pubmed/9295278 Culotta et al. (1997)].






Human basic fibroblast growth factor, bFGF

[http://partsregistry.org/Part:BBa_K380006 Part:BBa_K380006]


3D structure of bFGF. Primary citation [http://www.ncbi.nlm.nih.gov/pubmed/20133753 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 [http://www.ncbi.nlm.nih.gov/protein/153285461?report=fasta bFGF]


GenBank:

First reported by:





Protein A, z domain

[http://partsregistry.org/Part:BBa_K380009 Part:BBa_K380009]


[[Image:|300px|thumb|right|]]


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


GenBank:

First reported by:






IgG protease, IdeS

[http://partsregistry.org/Part:BBa_K380010 Part:BBa_K380010]


3D structure of IdeS. Primary citation [http://www.ncbi.nlm.nih.gov/pubmed/15574492 Wenig et al. 2004]


Gene (cDNA)
length 930 bp
removed restriction sites -
exchanged nt -
Protein
length 339 aa
size 37,977 Da
Fasta [http://www.ncbi.nlm.nih.gov/protein/209559219?report=fasta IdeS]


GenBank:

First reported by:







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