Article ; Online: Prediction of the binding location between the nuclear inhibitor of DNA binding and differentiation 2 (ID2) and HSPA5.
Pathology, research and practice
2024 Volume 255, Page(s) 155217
Abstract: Glucose-regulated protein 78 (GRP78), also termed HSPA5, was widely studied in cancer. It was recently approved that GRP78 has nuclear localization potential that sheds light on its role in cancer development. The inhibitor of DNA binding and ... ...
Abstract | Glucose-regulated protein 78 (GRP78), also termed HSPA5, was widely studied in cancer. It was recently approved that GRP78 has nuclear localization potential that sheds light on its role in cancer development. The inhibitor of DNA binding and differentiation 2 (ID2) is the nuclear component that associates with GRP78. The interaction between these two proteins is not understood clearly. In the current study, the binding pattern of GRP78/ID2 is predicted using computational methods. Protein-protein docking is used along with molecular dynamics simulation. The substrate binding domain β of GRP78 can stably interact with the loop region (C42-S60) of ID2 as predicted in this study. This paves the way for a possible destabilizer for this association and cancer eradication. |
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MeSH term(s) | Humans ; DNA ; Endoplasmic Reticulum Chaperone BiP/metabolism ; Inhibitor of Differentiation Protein 2/metabolism ; Neoplasms/metabolism ; Proteins |
Chemical Substances | DNA (9007-49-2) ; Endoplasmic Reticulum Chaperone BiP ; ID2 protein, human ; Inhibitor of Differentiation Protein 2 ; Proteins ; HSPA5 protein, human |
Language | English |
Publishing date | 2024-02-17 |
Publishing country | Germany |
Document type | Journal Article |
ZDB-ID | 391889-0 |
ISSN | 1618-0631 ; 0344-0338 |
ISSN (online) | 1618-0631 |
ISSN | 0344-0338 |
DOI | 10.1016/j.prp.2024.155217 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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