a tool for identifying drug-targetable redox-active disulphides

Major prion protein

Intermolecular

Cysteine 179 and cysteine 179

Cysteine 179 and cysteine 214

Cysteine 213 and cysteine 213

Intramolecular

Cysteine 179 and cysteine 214

Cysteine 166 and cysteine 221

A redox-regulated disulphide may form between two units of Major prion protein at cysteines 179 and 179.

Details

Redox score ?

65

PDB code

Structure name

infectious mammalian prion fibril (263k scrapie)

Structure deposition date

2021-02-06

Thiol separation (Å)

5

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Major prion protein

Peptide B name

Major prion protein

Peptide A accession

Peptide B accession

Peptide A residue number

179

Peptide B residue number

179

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Major prion protein at cysteines 179 and 214. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

40

PDB code

Structure name

infectious mammalian prion fibril (263k scrapie)

Structure deposition date

2021-02-06

Thiol separation (Å)

10

Half-sphere exposure sum ?

62

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Major prion protein

Peptide B name

Major prion protein

Peptide A accession

Peptide B accession

Peptide A residue number

179

Peptide B residue number

214

Ligandability

Cysteine 179 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 214 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Major prion protein at cysteines 213 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

31

PDB code

Structure name

arml prion fibril

Structure deposition date

2021-12-30

Thiol separation (Å)

10

Half-sphere exposure sum ?

85

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Major prion protein

Peptide B name

Major prion protein

Peptide A accession

Peptide B accession

Peptide A residue number

213

Peptide B residue number

213

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Major prion protein between cysteines 179 and 214.

Details

Redox score ?

80

PDB code

Structure name

human prion protein variant m166v

Structure deposition date

2000-05-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

79

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

179

Residue number B

214

Peptide name

Major prion protein

Ligandability

Cysteine 179 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 214 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Major prion protein between cysteines 166 and 221.

Details

Redox score ?

nan

PDB code

Structure name

human prion protein 121-230 m166c/e221c

Structure deposition date

2002-06-24

Thiol separation (Å)

2

Half-sphere exposure sum ?

44

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

166

Residue number B

221

Peptide name

Major prion protein

Ligandability

Cysteine 166 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 221 of Major prion protein

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 166 in protein A could not be asigned to a Uniprot residue.

Cysteine 221 in protein B could not be asigned to a Uniprot residue.

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