Related ArticlesNMR structure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins.
FEBS J. 2015 Jan;282(2):341-60
Authors: Carbajo RJ, Sanz L, Perez A, Calvete JJ
Abstract
Extant disintegrins, as found in the venoms of Viperidae and Crotalidae snakes (vipers and rattlesnakes, represent a family of polypeptides that block the function of ?1 and ?3 integrin receptors, both potently and with a high degree of selectivity. This toxin family owes its origin to the neofunctionalization of the extracellular region of an ADAM (a disintegrin and metalloprotease) molecule recruited into the snake venom gland proteome in the Jurassic. The evolutionary structural diversification of the disintegrin scaffold, from the ancestral long disintegrins to the more recently evolved medium-sized, dimeric and short disintegrins, involved the stepwise loss of pairs of class-specific disulfide linkages and the processing of the N-terminal region. NMR and crystal structures of medium-sized, dimeric and short disintegrins have been solved. However, the structure of a long disintegrin remained unknown. The present study reports the NMR solution structures of two disulfide bond conformers of the long disintegrin bitistatin from the African puff adder Bitis arietans. The findings provide insight into how a structural domain of the extracellular region of an ADAM molecule, recruited into and selectively expressed in the snake venom gland proteome as a PIII metalloprotease in the Jurassic, has subsequently been tranformed into a family of integrin receptor antagonists.
[Question from NMRWiki Q&A forum] using chenomx and missing peaks
using chenomx and missing peaks
hello, I am trying to identify and quantify of metabolites present in semen with spectra obtained from 400 MHz NMR using chenomx software. I have fit about 43 metabolites. I am sure that we must have ATP in our samples but it can not be fit and clusters in 6.1, 8.3 and 8.5 have been missed. So I am not sure about my results and I don't know what has happened. thank you for your answer.
Check if somebody has answered this question on NMRWiki QA forum
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01-07-2014 11:16 PM
[NMR paper] Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
Related Articles Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
J Biomol Struct Dyn. 2013 Jun 3;
Authors: Mahajan S, de Brevern AG, Offmann B, Srinivasan N
Abstract
Conformational changes in proteins are extremely important for their biochemical functions. Correlation between inherent conformational...
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06-05-2013 06:53 PM
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-29-2011 04:45 AM
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
[NMR paper] Three-dimensional structure of the RGD-containing snake toxin albolabrin in solution,
Three-dimensional structure of the RGD-containing snake toxin albolabrin in solution, based on 1H NMR spectroscopy and simulated annealing calculations.
Related Articles Three-dimensional structure of the RGD-containing snake toxin albolabrin in solution, based on 1H NMR spectroscopy and simulated annealing calculations.
Int J Pept Protein Res. 1996 Sep;48(3):220-8
Authors: Smith KJ, Jaseja M, Lu X, Williams JA, Hyde EI, Trayer IP
Albolabrin is a snake toxin that contains a RGD-(Arg-Gly-Asp) sequence motif and competes with fibrinogen to bind...
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08-22-2010 02:20 PM
[NMR paper] Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Related Articles Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Biochemistry. 1991 Dec 17;30(50):11625-36
Authors: Chen Y, Pitzenberger SM, Garsky VM, Lumma PK, Sanyal G, Baum J
The snake venom protein echistatin is a potent inhibitor of platelet aggregation. The inhibitory properties of echistatin have been attributed to the Arg-Gly-Asp sequence at residues 24-26. In this paper, sequence-specific nuclear magnetic...
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08-21-2010 11:12 PM
[NMR paper] Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Related Articles Proton NMR assignments and secondary structure of the snake venom protein echistatin.
Biochemistry. 1991 Dec 17;30(50):11625-36
Authors: Chen Y, Pitzenberger SM, Garsky VM, Lumma PK, Sanyal G, Baum J
The snake venom protein echistatin is a potent inhibitor of platelet aggregation. The inhibitory properties of echistatin have been attributed to the Arg-Gly-Asp sequence at residues 24-26. In this paper, sequence-specific nuclear magnetic...
NMR structure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins.
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