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-Structure paper
Title | Entropy of stapled peptide inhibitors in free state is the major contributor to the improvement of binding affinity with the GK domain. |
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Journal, issue, pages | Rsc Chem Biol, Vol. 2, Page 1274-1284, Year 2021 |
Publish date | Jun 29, 2021 (structure data deposition date) |
![]() | Unarta, I.C. / Xu, J. / Shang, Y. / Cheung, C.H.P. / Zhu, R. / Chen, X. / Cao, S. / Cheung, P.P. / Bierer, D. / Zhang, M. ...Unarta, I.C. / Xu, J. / Shang, Y. / Cheung, C.H.P. / Zhu, R. / Chen, X. / Cao, S. / Cheung, P.P. / Bierer, D. / Zhang, M. / Huang, X. / Li, X. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.446 - 2.595 Å |
Structure data | ![]() PDB-7f7g: ![]() PDB-7f7i: |
Chemicals | ![]() ChemComp-HOH: |
Source |
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![]() | PEPTIDE BINDING PROTEIN / MAGUK DLG stapled peptide linear peptide / MAGUK Stapled peptide entropy GK domain |