Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1
| Autor: | Johan Wouters, Manon Mirgaux, Laurence Leherte |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
3-dioxygenase-1
Stereochemistry Heme Crystal structure Crystallography X-Ray 010402 general chemistry Molecular Dynamics 01 natural sciences Cofactor Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Molecular dynamics Structural Biology Catalytic Domain Humans Indoleamine-Pyrrole 2 3 -Dioxygenase Indoleamine 2 3-dioxygenase tryptophan metabolism 030304 developmental biology 0303 health sciences Binding Sites cancer immunotherapy biology Chemistry JK-loop conformation Substrate (chemistry) Active site 0104 chemical sciences Loop (topology) biology.protein human indoleamine-2 3-dioxygenase-1 human indoleamine-2 |
| Zdroj: | Mirgaux, M, Leherte, L & Wouters, J 2020, ' Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1 ', Acta crystallographica. Section D: Structural Biology, vol. 76, pp. 1211-1221 . https://doi.org/10.1107/S2059798320013510 |
| Popis: | Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutictarget in cancer research. Its structure includes a loop, named the JK-loop, thatcontrols the orientation of the substrate or inhibitor within the active site.However, little has been reported about the crystal structure of this loop. In thepresent work, the conformation of the JK-loop is determined for the first time inthe presence of the heme cofactor in the active site through X-ray diffractionexperiments (2.44 A ˚ resolution). Molecular-dynamics trajectories were alsoobtained to provide dynamic information about the loop according to thepresence of cofactor. This new structural and dynamic information highlights theimportance of the JK-loop in confining the labile heme cofactor to the activesite. |
| Databáze: | OpenAIRE |
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