3G7C
Structure of the Phosphorylation Mimetic of Occludin C-term Tail
Summary for 3G7C
| Entry DOI | 10.2210/pdb3g7c/pdb |
| Related | 1WPA 1XAW |
| Descriptor | Occludin (2 entities in total) |
| Functional Keywords | occludin, diabetic retinopathy, zo-1, tight junction, adhesion, cell junction, coiled coil, membrane, phosphoprotein, transmembrane, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13636.14 |
| Authors | Tash, B.R.,Sundstrom, J.M.,Murakami, T.,Flanagan, J.M.,Bewley, M.C.,Antonetii, D.A. (deposition date: 2009-02-09, release date: 2009-05-12, Last modification date: 2023-09-06) |
| Primary citation | Sundstrom, J.M.,Tash, B.R.,Murakami, T.,Flanagan, J.M.,Bewley, M.C.,Stanley, B.A.,Gonsar, K.B.,Antonetti, D.A. Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach. J.PROTEOME RES., 8:808-817, 2009 Cited by PubMed Abstract: The molecular function of occludin, an integral membrane component of tight junctions, remains unclear. VEGF-induced phosphorylation sites were mapped on occludin by combining MS data analysis with bioinformatics. In vivo phosphorylation of Ser490 was validated and protein interaction studies combined with crystal structure analysis suggest that Ser490 phosphorylation attenuates the interaction between occludin and ZO-1. This study demonstrates that combining MS data and bioinformatics can successfully identify novel phosphorylation sites from limiting samples. PubMed: 19125584DOI: 10.1021/pr7007913 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
