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.

TLDR
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

TLDR
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.

TLDR
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

TLDR
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

TLDR
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.

TLDR
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.

Elucidation of the disulfide‐folding pathway of hirudin by a topology‐based approach

TLDR
The model possesses the minimal ingredients necessary to investigate the much debated issue of whether the refolding process occurs through partially structured intermediates with native or non‐native disulfide bonds, and can be tuned to reproduce well a set of experimental transitions between species with different number of formed disulfides.

Modularity in the TNF-receptor family.

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