1H‐NMR studies and secondary structure of the RGD‐containing snake toxin, albolabrin
- 1 December 1993
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 218 (3), 853-860
- https://doi.org/10.1111/j.1432-1033.1993.tb18441.x
Abstract
Albolabrin is a naturally occurring peptide from snake venom containing the sequence Arg-Gly-Asp (RGD). It inhibits platelet aggregation by blocking the binding of fibrinogen to the glycoprotein Gp IIb-IIIa, on the surface of activated platelets. Albolabrin consists of 73 residues with six intramolecular disulphide bonds. The 1H-NMR spectrum of albolabrin has been assigned using homonuclear two-dimensional techniques and its secondary structure determined. Like kistrin and echistatin, two related peptides from snake venom, albolabrin appears to have little regular secondary structure in solution. Several bends and two short distorted beta sheets are observed. The RGD sequence, important for binding to the receptor, lies in a mobile loop joining two strands of one of these beta sheets. This loop undergoes a pH-dependent conformational change.Keywords
This publication has 35 references indexed in Scilit:
- Determination of the Disulphide Bonding Pattern in Proteins by Local and Global Analysis of Nuclear Magnetic Resonance DataJournal of Molecular Biology, 1993
- Cysteine pairing in the glycoprotien IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculationsBiochemistry, 1993
- The solution structure of echistatin: evidence for disulphide bond rearrangement in homologous snake toxinsProtein Engineering, Design and Selection, 1992
- Elegantin and albolabrin purified peptides from viper venoms; homologies with the RGDS domain of fibrinogen and von Willebrand factorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopyJournal of Magnetic Resonance (1969), 1985
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Coherence transfer by isotropic mixing: Application to proton correlation spectroscopyJournal of Magnetic Resonance (1969), 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Simplification of NMR spectra by filtration through multiple-quantum coherenceJournal of Magnetic Resonance (1969), 1983
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980