A disulphide-reinforced structural scaffold shared by small proteins with diverse functions

@article{Lin1995ADS,
  title={A disulphide-reinforced structural scaffold shared by small proteins with diverse functions},
  author={Shuo-liang Lin and Ruth Nussinov},
  journal={Nature Structural Biology},
  year={1995},
  volume={2},
  pages={835-837}
}
We describe the T-knot scaffold, a structural feature shared by the EGF-like proteins, alpha-toxins and proteinase inhibitors from plants. 

The hairpin stack fold, a novel protein architecture for a new family of protein growth factors

The granulin/epithelin protein motif has an unusual structure consisting of a parallel stack of β-hairpins stapled together by six disulphide bonds. The new structure also contains a folding

The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides.

These results demonstrate that E.coli cell surface display of conformationally constrained peptides tethered to the EETI-II cystine knot scaffold has the potential to become an effective technique for the rapid isolation of small peptide molecules from combinatorial libraries that bind with high affinity to acceptor molecules.

The T-Knot Motif Revisited

It is suggested that folding and stability of the T-knot scaffold mainly depend on the geometry of the two knotted disulphides and on the loop length, and that the secondary structure elements are not a prerequisite for motif formation.

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge.

A family of insect-selective neurotoxins from the venom of the Australian funnel-web spider appears to be good candidates for biopesticide engineering and it is proposed that J-ACTX comprises an ancestral protein fold that is referred to as the disulfide-directed beta-hairpin.

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge

A family of insect-selective neurotoxins from the venom of the Australian funnel-web spider appears to be good candidates for biopesticide engineering and it is proposed that J-ACTX comprises an ancestral protein fold that is referred to as the disulfide-directed β-hairpin.

Structural determinants of mini‐protein stability

Strategies adopted by different classes of mini‐proteins to attain family‐characteristic, well‐ordered, three‐dimensional structures are reviewed.

Protein similarities beyond disulphide bridge topology.

A new approach and program, KNOT-MATCH, has been developed for automated structural superimposition of proteins by means of their disulphide bridge topology that can be very useful for finding relationships among proteins that would be hidden to the current alignment methods based on sequence and on main-chain topology.

Modularity in the TNF-receptor family.

Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking.

Experimental results show, surprisingly, that an interstrand disulfide bond can stabilize parallel β-sheets formed by an autonomously folding peptide in aqueous solution.

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