Related ArticlesNMR structural determination of viscotoxin A3 from Viscum album L.
Biochem J. 2000 Sep 1;350 Pt 2:569-77
Authors: Romagnoli S, Ugolini R, Fogolari F, Schaller G, Urech K, Giannattasio M, Ragona L, Molinari H
The high-resolution three-dimensional structure of the plant toxin viscotoxin A3, from Viscum album L., has been determined in solution by (1)H NMR spectroscopy at pH 3.6 and 12 degrees C (the structure has been deposited in the Protein Data Bank under the id. code 1ED0). Experimentally derived restraints including 734 interproton distances from nuclear Overhauser effect measurements, 22 hydrogen bonds, 32 φ angle restraints from J coupling measurements, together with three disulphide bridge constraints were used as input in restrained molecular dynamics, followed by minimization, using DYANA and Discover. Backbone and heavy atom root-mean-square deviations were 0.47+/-0.11 A (1 A=10(-10) m) and 0.85+/-0.13 A respectively. Viscotoxin A3 consists of two alpha-helices connected by a turn and a short stretch of antiparallel beta-sheet. This fold is similar to that found in other thionins, such as crambin, hordothionin-alpha and -beta, phoratoxin A and purothionin-alpha and -beta. The difference in the observed biological activity for thionins of known structure is discussed in terms of the differences in the calculated surface potential distribution, playing an important role in their function through disruption of cell membranes. In addition, the possible role in DNA binding of the helix-turn-helix motif of viscotoxin A3 is discussed.
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
The New York Structural Biology Center (NYSBC) seeks an experienced electron microscopist to join the staff of its Cryo-Electron Microscope Facility (http://cryoem.nysbc.org). The NYSBC is shared center that supports state-of-the-art research in cryo-EM, NMR, and X-ray. Cryo-EM facilities include four transmission electron microscopes and a new d...
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[NMR paper] Structural determination of the active site of a sweet protein. A 1H NMR investigatio
Structural determination of the active site of a sweet protein. A 1H NMR investigation of pMNEI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural determination of the active site of a sweet protein. A 1H NMR investigation of pMNEI.
FEBS Lett. 1992 Sep 21;310(1):27-30
Authors: Tancredi T, Iijima H, Saviano G, Amodeo P, Temussi PA
pMNEI, a single chain sweet protein related to monellin, has been studied by means of 1H NMR at 500 MHz. A partial sequential...
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[NMR paper] Determination of the secondary structural elements of chicken liver fatty acid bindin
Determination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Determination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.
Biopolymers. 1999 Jul;50(1):1-11
Authors: Schievano E, Mammi S, Peggion E
A conformational study in solution of the fatty acid...
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Structural determination of biomolecular interfaces by nuclear magnetic resonance of
Abstract Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation. Although powerful, these techniques cannot provide unambiguous estimates of intermolecular distances between interacting proteins. Here, we present an alternative approach, called REDSPRINT (REDduced/Standard PRoton density INTerface identification), to map protein interfaces with...
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Precise structural determination of weakly binding peptides by utilizing dihedral ang
Abstract Structural determination of target-bound conformations of peptides is of primary importance for the optimization of peptide ligands and peptideā??mimetic design. In the structural determination of weakly binding ligands, transferred nuclear Overhauser effect (TrNOE) methods have been widely used. However, not many distance constraints can be obtained from small peptide ligands by TrNOE, especially for peptides bound to a target molecule in an extended conformation. Therefore, for precise structural determination of weakly binding peptides, additional structural constraints are...
NMR structural determination of viscotoxin A3 from Viscum album L.
Linear Mode
