Related ArticlesNMR structural studies of human cystatin C dimers and monomers.
J Mol Biol. 1997 Aug 15;271(2):266-77
Authors: Ekiel I, Abrahamson M, Fulton DB, Lindahl P, Storer AC, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, LeSauteur L, Gehring K
Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity as a cysteine proteinase inhibitor. A similar process of dimerization has been observed in cells, and may be related to the amyloid formation seen for the L68Q variant of the protein. Dimerization is barrier controlled, and no dimer/monomer interconversion can be observed at physiological conditions. As a consequence, very stable, "trapped" dimers can be easily separated from monomers. A study of the structural aspects of cystatin C dimer formation was undertaken using NMR spectroscopy. The monomer/dimer model was verified by (pulse field gradient NMR) self-diffusion molecular mass measurements. Complete backbone resonance assignments and secondary structure determination were obtained for the monomer using data from triple resonance experiments performed on 13C/15N doubly labeled protein. A marked similarity of the cystatin C secondary structure to that of chicken cystatin was observed. Using uniformly and amino-acid-specific 15N-enriched protein, backbone NH signals were assigned for cystatin C in its dimeric state. Comparison of 1H -15N correlation NMR spectra of the monomer and dimer shows that the three-dimensional structure remains unchanged in the dimer and that only local perturbations occur. These are localized to the amino acid residues comprising the cysteine proteinase binding site. Such a mode of dimerization readily explains the complete loss of the inhibitory activity in the dimer. The NMR results also demonstrate that the dimer is symmetric.
NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions.
NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions.
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J Phys Chem B. 2010 Dec 2;
Authors: Barhoum S, Yethiraj A
Protein aggregation is an important biophysical phenomenon, and it is technically challenging to quantify. Scattering studies in concentrated protein solutions are not in complete agreement over the existence of an equilibrium cluster phase. We use...
[NMR paper] Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor:
Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study.
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Biochim Biophys Acta. 2004 May 27;1663(1-2):74-81
Authors: Katragadda M, Maciejewski MW, Yeagle PL
The recently reported crystal structure of bovine rhodopsin revealed a cytoplasmic helix (helix 8) in addition to the seven transmembrane helices. This domain is roughly perpendicular to the transmembrane bundle in the presence of an...
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[NMR paper] What function for human lithostathine?: structural investigations by three-dimensiona
What function for human lithostathine?: structural investigations by three-dimensional structure modeling and high-resolution NMR spectroscopy.
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Protein Eng. 1996 Nov;9(11):949-57
Authors: Patard L, Stoven V, Gharib B, Bontems F, Lallemand JY, De Reggi M
Human lithostathine is a 144-residue protein, expressed in various organs and pathologies. Several biological functions have been...
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[NMR paper] NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural inf
NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
Eur J Biochem. 1996 Oct 1;241(1):229-42
Authors: ...
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[NMR paper] Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectro
Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A.
Related Articles Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A.
Biochemistry. 1995 Nov 14;34(45):14637-48
Authors: Tate S, Ushioda T, Utsunomiya-Tate N, Shibuya K, Ohyama Y, Nakano Y,...
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[NMR paper] A calculation strategy for the structure determination of symmetric dimers by 1H NMR.
A calculation strategy for the structure determination of symmetric dimers by 1H NMR.
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Proteins. 1993 Nov;17(3):297-309
Authors: Nilges M
The structure determination of symmetric dimers by NMR is impeded by the ambiguity of inter- and intramonomer NOE crosspeaks. In this paper, a calculation strategy is presented that allows the calculation of dimer structures without resolving the ambiguity by additional experiments (like asymmetric...
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[NMR paper] NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-ma
NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
Related Articles NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
J Biol Chem. 1990 May 5;265(13):7268-72
Authors: Gettins P, Sottrup-Jensen L
NMR and ESR spectroscopies have been used to examine the plasma protease inhibitor pregnancy zone protein (PZP) and its complex with chymotrypsin. The 1H NMR spectrum of PZP shows relatively few sharp resonances, which, by analogy with human alpha...
NMR structural studies of human cystatin C dimers and monomers.
Linear Mode
