1mmc

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmc OCA], [http://www.ebi.ac.uk/pdbsum/1mmc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mmc RCSB]</span>
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'''1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2'''
'''1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2'''
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[[Category: Willem, R.]]
[[Category: Willem, R.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
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[[Category: antifungal antimicrobial]]
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[[Category: Antifungal antimicrobial]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:24:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:02 2008''
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Revision as of 22:24, 2 May 2008

Template:STRUCTURE 1mmc

1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2


Overview

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.

About this Structure

1MMC is a Single protein structure of sequence from Amaranthus caudatus. Full crystallographic information is available from OCA.

Reference

H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus., Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P, J Mol Biol. 1996 May 3;258(2):322-33. PMID:8627629 Page seeded by OCA on Sat May 3 01:24:57 2008

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