Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules.
- BiologyMolecular endocrinology
They are absent in the unicellular yeast genome but present in nematode, fly, and higher species, indicating that the cystine knot structure evolved in extracellular signaling molecules of multicellular organisms.
Molecular architecture and biorecognition processes of the cystine knot protein superfamily: part I. The glycoprotein hormones
- Biology, ChemistryJournal of molecular recognition : JMR
This review article focuses on the structural motifs involved in receptor recognition and the current techniques available to identify these regions, including the role of immunological methodology, peptide fragment design and synthesis and mutagenesis to delineate their structure–function relationships and molecular recognition behaviour.
The cystine knot structure of ion channel toxins and related polypeptides.
- BiologyToxicon : official journal of the International Society on Toxinology
Oxidative folding of cyclic cystine knot proteins.
- Biology, ChemistryAntioxidants & redox signaling
The points summarized in this review will be important to consider in the design of novel pharmaceutically interesting biomolecules based on the cyclic cystine knot motif, which has shown potential as a molecular scaffold because of its exceptional stability.
Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity.
- Chemistry, BiologyJournal of molecular biology
The three-dimensional solution structure of circulin A, a 30 residue polypeptide from the African plant Chassalia parvifolia, has been determined using two-dimensional 1H-NMR spectroscopy and provides additional evidence for a solvent-exposed Trp residue.
Molecular modelling of the Norrie disease protein predicts a cystine knot growth factor tertiary structure
- BiologyNature Genetics
This model identifies Norrie disease protein (NDP) as a member of an emerging family of growth factors containing a cystine knot motif, with direct implications for the physiological role of NDP.
Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.
- Biology, ChemistryJournal of molecular biology
The structural features of the two apparent subfamilies of the CCK peptides which may be significant for the likely defense related role of these peptides within plants are defined.
Acyclic Permutants of Naturally Occurring Cyclic Proteins
- Biology, ChemistryThe Journal of Biological Chemistry
The complete suite of acyclic permutants of kalata B1 are synthesized and it is shown that it is possible to disrupt regions of the β-sheet and still allow folding into native-like structure, provided the cystine knot is intact.
Topological similarities in TGF-beta 2, PDGF-BB and NGF define a superfamily of polypeptide growth factors.
Diversity in the disulfide folding pathways of cystine knot peptides
- BiologyLetters in Peptide Science
This work has examined the oxidative refolding and reductive unfolding of the prototypic member of the cyclotide family, kalata B1, suggesting that the circular backbone has a significant influence in directing the folding pathway.
SHOWING 1-10 OF 24 REFERENCES
Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.
Sequence profile analysis of other members of the TGF-beta superfamily, including the activins, inhibins, and several developmental factors, imply that they also adopt the T GF-beta fold.
New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor
- Biology, ChemistryNature
The crystal structure of the murine NGF dimer is reported, which reveals a novel protomer structure consisting of three antiparallel pairs of β strands, together forming a flat surface that provides a model for rational design of analogues of NGF and its relatives and for testing the NGF-receptor recognition determinants critical for signal transduction.
An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth fact or-β2
The crystal structure of TGF-β2 is reported at 2.2 Å resolution, which reveals a novel monomer fold and dimer association and provides a suitable model for the T GF-βs and other members of the super-family9–11 and is the basis for the analysis of the TGF -β2 interactions with the receptor.
Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.
Examination of the 2.8 angstrom crystal structure of the complex between the hormone and the extracellular domain of its receptor (hGHbp) showed that the complex consists of one molecule of growth hormone per two molecules of receptor.
Two PDGF‐B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation.
- Biology, ChemistryThe EMBO journal
Two critical amino acid residues in PDGF‐B chain residues, arginine 27 and isoleucine 30, have been identified by a site‐directed mutagenesis programme and circular dichroism and fluorescence spectroscopy show that such mutations do not disrupt the structure of PDGF.
Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF.
- Biology, ChemistryThe Journal of biological chemistry
Five PDGF B amino acid substitutions convert PDGF A to a PDGF B-like transforming molecule.
- BiologyThe Journal of biological chemistry
Crystal structure of human platelet‐derived growth factor BB.
- ChemistryThe EMBO journal
The crystal structure of the homodimeric BB isoform of human recombinant platelet-derived growth factor (PDGF-BB) has been determined by X-ray analysis to 3.0 A resolution and it is shown that dimerization leads to the clustering of three surface loops at each end of the elongated dimer, which most probably form the receptor recognition sites.