| First Author | Zhang W | Year | 2009 |
| Journal | Genes Dev | Volume | 23 |
| Issue | 12 | Pages | 1387-92 |
| PubMed ID | 19528316 | Mgi Jnum | J:155180 |
| Mgi Id | MGI:4412430 | Doi | 10.1101/gad.1789209 |
| Citation | Zhang W, et al. (2009) Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione. Genes Dev 23(12):1387-92 |
| abstractText | Eukaryotic lanthionine synthetase C-like protein 1 (LanCL1) is homologous to prokaryotic lanthionine cyclases, yet its biochemical functions remain elusive. We report the crystal structures of human LanCL1, both free of and complexed with glutathione, revealing glutathione binding to a zinc ion at the putative active site formed by conserved GxxG motifs. We also demonstrate by in vitro affinity analysis that LanCL1 binds specifically to the SH3 domain of a signaling protein, Eps8. Importantly, expression of LanCL1 mutants defective in Eps8 interaction inhibits nerve growth factor (NGF)-induced neurite outgrowth, providing evidence for the biological significance of this novel interaction in cellular signaling and differentiation. |
