Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4EC7

Cobra NGF in complex with lipid

Summary for 4EC7
Entry DOI10.2210/pdb4ec7/pdb
DescriptorVenom nerve growth factor, (2S)-1-hydroxy-3-(tetradecanoyloxy)propan-2-yl docosanoate (3 entities in total)
Functional Keywordscobra ngf, unknown lipid, hormone
Biological sourceNaja atra (Chinese cobra)
Cellular locationSecreted: P61898
Total number of polymer chains2
Total formula weight26786.31
Authors
Jiang, T.,Wang, F.,Tong, Q. (deposition date: 2012-03-26, release date: 2012-09-12, Last modification date: 2024-11-13)
Primary citationTong, Q.,Wang, F.,Zhou, H.Z.,Sun, H.L.,Song, H.,Shu, Y.Y.,Gong, Y.,Zhang, W.T.,Cai, T.X.,Yang, F.Q.,Tang, J.,Jiang, T.
Structural and functional insights into lipid-bound nerve growth factors
Faseb J., 26:3811-3821, 2012
Cited by
PubMed Abstract: Nerve growth factor (NGF) is a dimeric molecule that modulates the survival, proliferation, and differentiation of nervous cells and is also known to act on cells of the immune system and endocrine system. NGFs extracted from mouse submaxillary gland and cobra venom have different immunological behaviors, yet the underlying mechanism remains unclear. Here we report the crystal structure of the NGF purified from Chinese cobra Naja naja atra (cNGF), which unexpectedly reveals a 2-tailed lipid molecule that is embedded between the two protomers of the NGF homodimer. In addition, crystallographic analysis indicated that the purified mouse NGF(mNGF) is free from lipid but can bind lysophosphatidylserine (lyso-PS) in the same pocket as cNGF. Bioassays indicated that the binding of lipid molecules to cNGF and mNGF are essential for their mast cell activation activity and abates their p75(NTR) binding capacity. Taken together, these results suggest a new mechanism for the regulation of the function of NGF.
PubMed: 22649032
DOI: 10.1096/fj.12-207316
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

237992

數據於2025-06-25公開中

PDB statisticsPDBj update infoContact PDBjnumon