PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study
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PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study Descriptor: D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, Fibroblast growth factor 2 Authors: Tsao, Y.H. Deposit date: 2017-01-26 Release date: 2018-03-07 Last modified: 2024-10-30 Method: X-RAY DIFFRACTION (1.9 Å) Cite: PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study To Be Published
创建时间:
2017-01-26



