| Structural highlights
2wfj is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| NonStd Res: | , , , , , |
| Related: | 2gw2, 2wfi, 1bck, 1c5f, 1csa, 1cwa, 1cwb, 1cwc, 1cwf, 1cwh, 1cwi, 1cwj, 1cwk, 1cwl, 1cwm, 1cwo, 1cya, 1cyb, 1cyn, 1ikf, 1m63, 1mf8, 1mik, 1qng, 1qnh, 1xq7, 2esl, 2oju, 2poy, 2rma, 2rmb, 2rmc, 2x2c, 2x7k, 2z6w, 3bo7, 3cys, 3eov |
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
Publication Abstract from PubMed
Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction.
The thermodynamic influence of trapped water molecules on a protein-ligand interaction.,Stegmann CM, Seeliger D, Sheldrick GM, de Groot BL, Wahl MC Angew Chem Int Ed Engl. 2009;48(28):5207-10. PMID:19499554[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stegmann CM, Seeliger D, Sheldrick GM, de Groot BL, Wahl MC. The thermodynamic influence of trapped water molecules on a protein-ligand interaction. Angew Chem Int Ed Engl. 2009;48(28):5207-10. PMID:19499554 doi:10.1002/anie.200900481
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