1cjp

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[[Image:1cjp.gif|left|200px]]
[[Image:1cjp.gif|left|200px]]
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{{Structure
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|PDB= 1cjp |SIZE=350|CAPTION= <scene name='initialview01'>1cjp</scene>, resolution 2.78&Aring;
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The line below this paragraph, containing "STRUCTURE_1cjp", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MUG:4-METHYLUMBELLIFERYL-ALPHA-D-GLUCOSE'>MUG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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{{STRUCTURE_1cjp| PDB=1cjp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjp OCA], [http://www.ebi.ac.uk/pdbsum/1cjp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cjp RCSB]</span>
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}}
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'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE'''
'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE'''
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[[Category: Kanellopoulos, P N.]]
[[Category: Kanellopoulos, P N.]]
[[Category: Tucker, P A.]]
[[Category: Tucker, P A.]]
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[[Category: legume lectin]]
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[[Category: Legume lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:48:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:22:56 2008''
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Revision as of 09:48, 2 May 2008

Template:STRUCTURE 1cjp

CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE


Overview

Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides.

About this Structure

1CJP is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

Reference

The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:9087912 Page seeded by OCA on Fri May 2 12:48:22 2008

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