2gw2
Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin GCrystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G
Structural highlights
Function[PPIG_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
|
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Peptidylprolyl isomerase
- Arrowsmith, C H
- Bernstein, G
- Bochkarev, A
- Davis, T
- Dhe-Paganon, S
- Edwards, A M
- Finerty, P J
- Mackenzie, F
- Newman, E M
- Structural genomic
- Sundstrom, M
- Tempel, W
- Weigelt, J
- Cis-trans isomerization
- Isomerase
- Mutant
- Mutation
- Peptidyl-prolyl isomerase
- Ppiase
- Protein folding
- Sgc
- Surface mutagenesis