Related ArticlesCharacterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.
Protein Sci. 1995 Jun;4(6):1045-55
Authors: Wimberly B, Thulin E, Chazin WJ
Calbindin D9k is a small EF-hand protein that binds two calcium ions with positive cooperativity. The molecular basis of cooperativity for the binding pathway where the first ion binds in the N-terminal site (1) is investigated by NMR experiments on the half-saturated state of the N56A mutant, which exhibits sequential yet cooperative binding (Linse S, Chazin WJ, 1995, Protein Sci 4:1038-1044). Analysis of calcium-induced changes in chemical shifts, amide proton exchange rates, and NOEs indicates that ion binding to the N-terminal binding loop causes significant changes in conformation and/or dynamics throughout the protein. In particular, all three parameters indicate that the hydrophobic core undergoes a change in packing to a conformation very similar to the calcium-loaded state. These results are similar to those observed for the (Cd2+)1 state of the wild-type protein, a model for the complementary half-saturated state with an ion bound in the C-terminal site (II). Thus, with respect to cooperativity in either of the binding pathways, binding of the first ion drives the conformation and dynamics of the protein far toward the (Ca2+)2 state, thereby facilitating binding of the second ion. Comparison with the half-saturated state of the analogous E65Q mutant confirms that mutation of this critical bidentate calcium ligand at position 12 of the consensus EF-hand binding loop causes very significant structural perturbations. This result has important implications regarding numerous studies that have utilized mutation of this critical residue for site deactivation.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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09-30-2011 06:00 AM
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
[NMR paper] NMR characterization of the interaction between the C-terminal domain of interferon-g
NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Related Articles NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.
Biochem J. 2004 Nov 15;384(Pt 1):93-9
Authors: Vanhaverbeke C, Simorre JP, Sadir R, Gans P, Lortat-Jacob H
Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNgamma (interferon-gamma) is secreted by activated T-cells and...
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11-24-2010 10:03 PM
[NMR paper] Low temperature solid-state NMR experiments of half-integer quadrupolar nuclides: cav
Low temperature solid-state NMR experiments of half-integer quadrupolar nuclides: caveats and data analysis.
Related Articles Low temperature solid-state NMR experiments of half-integer quadrupolar nuclides: caveats and data analysis.
J Magn Reson. 2004 May;168(1):66-74
Authors: Lipton AS, Heck RW, Sears JA, Ellis PD
Solid-state NMR spectroscopy of half-integer quadrupolar nuclides has received a lot of interest recently with the advent of new methodologies and higher magnetic fields. We present here the extension of our previous low...
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11-24-2010 09:51 PM
[NMR paper] NMR structural characterization of the N-terminal domain of the adenylyl cyclase-asso
NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
Related Articles NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
J Biomol NMR. 2004 May;29(1):73-84
Authors: Mavoungou C, Israel L, Rehm T, Ksiazek D, Krajewski M, Popowicz G, Noegel AA, Schleicher M, Holak TA
Cyclase-associated proteins (CAPs) are highly conserved, ubiquitous actin binding proteins that are involved in...
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[NMR paper] Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Biochemistry. 2003 Feb 18;42(6):1460-9
Authors: Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG
FCP1 (TFIIF-associated CTD phosphatase) is the only known phosphatase specific for the phosphorylated CTD of RNAP II. The phosphatase activity of FCP1 is...
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[NMR paper] NMR solution structure of calcium-saturated skeletal muscle troponin C.
NMR solution structure of calcium-saturated skeletal muscle troponin C.
Related Articles NMR solution structure of calcium-saturated skeletal muscle troponin C.
Biochemistry. 1995 Dec 12;34(49):15953-64
Authors: Slupsky CM, Sykes BD
Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution...
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[U. of Ottawa NMR Facility Blog] Solid State NMR of Half Integer Quadrupolar Nuclei
Solid State NMR of Half Integer Quadrupolar Nuclei
Many students who do liquid state NMR or solid state NMR of spin I=1/2 nuclei have very little appreciation for the information content and complexity of the solid state NMR spectra of spin I = n/2 quadrupolar nuclei (n= 3, 5, 7....). In part, I think this may be due to the mathematics involved with explaining the important effects. With this post, I attempt to describe the NMR spectrum of an I = 5/2 nucleus in the soild state without resorting to mathematics. I hope that this post helps to boost the understanding and appreciation for the...