1mmc
From Proteopedia
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| - | [[Image:1mmc.gif|left|200px]] | + | [[Image:1mmc.gif|left|200px]] |
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| - | '''1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2''' | + | {{Structure |
| + | |PDB= 1mmc |SIZE=350|CAPTION= <scene name='initialview01'>1mmc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MMC is a [ | + | 1MMC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Amaranthus_caudatus Amaranthus caudatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8627629 8627629] |
[[Category: Amaranthus caudatus]] | [[Category: Amaranthus caudatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: antifungal antimicrobial]] | [[Category: antifungal antimicrobial]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:17 2008'' |
Revision as of 10:45, 20 March 2008
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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 Thu Mar 20 12:45:17 2008
