3e73 | pdb_00003e73

Crystal Structure of Human LanCL1 complexed with GSH

spinqualitylabelsall models 3e73, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e73 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: GSH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LANC1_HUMAN May play a role in EPS8 signaling. Binds glutathion. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione.,Zhang W, Wang L, Liu Y, Xu J, Zhu G, Cang H, Li X, Bartlam M, Hensley K, Li G, Rao Z, Zhang XC Genes Dev. 2009 Jun 15;23(12):1387-92. PMID:19528316 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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