Related ArticlesH NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
J Mol Biol. 1996 May 3;258(2):322-33
Authors: Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P
The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein.
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[NMR paper] 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a suga
1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
FEBS Lett. 1995 Aug 21;370(3):245-9
Authors: Verheyden P, Pletinckx J, Maes D, Pepermans HA, Wyns L, Willem R, Martins JC
...
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The NMR solution structure of...
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Biochemistry. 1994 Apr 19;33(15):4721-9
Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...
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Biochemistry. 1992 Nov 3;31(43):10449-57
Authors: Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M
The structure of the B2 immunoglobulin-binding domain of streptococcal protein G has been determined at 1.67-A...
H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial prote
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