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5NGN

Lybatide 2, a cystine-rich peptide from Lycium barbarum

Summary for 5NGN
Entry DOI10.2210/pdb5ngn/pdb
Descriptorlybatide 2, GLYCEROL, ACETONITRILE, ... (5 entities in total)
Functional Keywordscysteine-rich peptide, pi-helix, wolfberry, disulfide bonds, plant protein
Biological sourceLycium barbarum (goji berry)
Total number of polymer chains3
Total formula weight11334.63
Authors
Lei, J.,Tan, W.L.,Sakai, N.,Hilgenfeld, R. (deposition date: 2017-03-18, release date: 2017-07-26, Last modification date: 2024-10-16)
Primary citationTan, W.L.,Wong, K.H.,Lei, J.,Sakai, N.,Tan, H.W.,Hilgenfeld, R.,Tam, J.P.
Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold.
Sci Rep, 7:5194-5194, 2017
Cited by
PubMed Abstract: Cysteine-rich peptides (CRPs) of 2-6 kDa are generally thermally and proteolytically stable because of their multiple cross-bracing disulfide bonds. Here, we report the discovery and characterization of two novel cystine-stapled CRPs, designated lybatide 1 and 2 (lyba1 and lyba2), from the cortex of Lycium barbarum root. Lybatides, 32 to 33 amino acids in length, are hyperstable and display a novel disulfide connectivity with a cysteine motif of C-C-C-C-CC-CC which contains two pairs of adjacent cysteines (-CC-CC). X-ray structure analysis revealed the presence of a single cystine-stabilized (α + π)-helix in lyba2, a rare feature of CRPs. Together, our results suggest that lybatides, one of the smallest four-disulfide-constrained plant CRPs, is a new family of CRPs. Additionally, this study provides new insights into the molecular diversity of plant cysteine-rich peptides and the unusual lybatide scaffold could be developed as a useful template for peptide engineering and therapeutic development.
PubMed: 28701689
DOI: 10.1038/s41598-017-05037-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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