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-Structure paper
Title | Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. U.S.A., Vol. 116, Page 2068-2077, Year 2019 |
Publish date | Apr 12, 2018 (structure data deposition date) |
![]() | Liu, X. / An, T. / Li, D. / Fan, Z. / Xiang, P. / Li, C. / Ju, W. / Li, J. / Hu, G. / Qin, B. ...Liu, X. / An, T. / Li, D. / Fan, Z. / Xiang, P. / Li, C. / Ju, W. / Li, J. / Hu, G. / Qin, B. / Yin, B. / Wojdyla, J.A. / Wang, M. / Yuan, J. / Qiang, B. / Shu, P. / Cui, S. / Peng, X. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.201 - 3.29 Å |
Structure data | ![]() PDB-5zo1: ![]() PDB-5zo2: |
Chemicals | ![]() ChemComp-GOL: ![]() ChemComp-HOH: |
Source |
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![]() | CELL ADHESION / cell adhesion molecule / glycoprotein / Ig-like domain / Necl4 / Necl / Nectin / Nectin-Like Molecules / CADM / Native-SAD / disulfide bridges / SynCAM4 / Schwann cell / myelogenesis / Ig domain / SynCam / Nectin-like / Necl-4 / Necl-1 / axon / Molecular Replacement / heterogeneous dimer |