3E6U
Crystal structure of Human LanCL1
Summary for 3E6U
Entry DOI | 10.2210/pdb3e6u/pdb |
Related | 3E73 |
Descriptor | LanC-like protein 1, ZINC ION (3 entities in total) |
Functional Keywords | alpha barrel, cytoplasm, signaling protein |
Biological source | Homo sapiens (Human) |
Cellular location | Cytoplasm: O43813 |
Total number of polymer chains | 4 |
Total formula weight | 187800.12 |
Authors | |
Primary citation | Zhang, W.,Wang, L.,Liu, Y.,Xu, J.,Zhu, G.,Cang, H.,Li, X.,Bartlam, M.,Hensley, K.,Li, G.,Rao, Z.,Zhang, X.C. Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione Genes Dev., 23:1387-1392, 2009 Cited by PubMed Abstract: 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. PubMed: 19528316DOI: 10.1101/gad.1789209 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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