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1jmm

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(New page: 200px<br /><applet load="1jmm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmm, resolution 2.40&Aring;" /> '''Crystal structure of...)
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caption="1jmm, resolution 2.40&Aring;" />
'''Crystal structure of the V-region of Streptococcus mutans antigen I/II'''<br />
'''Crystal structure of the V-region of Streptococcus mutans antigen I/II'''<br />
==Overview==
==Overview==
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Antigens I/II are large multifunctional adhesins from oral viridans, streptococci that exert immunomodulatory effects on human cells and play, important roles in inflammatory disorders. Among them, Streptococcus, mutans plays a major role in the initiation of dental caries. The, structure of the V-region (SrV+, residues 464-840) of the antigen I/II of, S. mutans has been determined using the multiwavelength anomalous, diffraction phasing technique with seleno-methionine-substituted, recombinant protein and subsequently refined at 2.4 A resolution. The, crystal structure of SrV+ revealed a lectin-like fold that displays a, putative preformed carbohydrate-binding site stabilized by a metal ion., Inhibition of this binding site may confer to humans a protection against, dental caries and dissemination of the bacteria to extra-oral sites, involved in life-threatening inflammatory diseases. This crystal structure, constitutes a first step in understanding the structure-function, relationship of antigens I/II and may help in delineating new preventive, or therapeutic strategies against colonization of the host by oral, streptococci.
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Antigens I/II are large multifunctional adhesins from oral viridans streptococci that exert immunomodulatory effects on human cells and play important roles in inflammatory disorders. Among them, Streptococcus mutans plays a major role in the initiation of dental caries. The structure of the V-region (SrV+, residues 464-840) of the antigen I/II of S. mutans has been determined using the multiwavelength anomalous diffraction phasing technique with seleno-methionine-substituted recombinant protein and subsequently refined at 2.4 A resolution. The crystal structure of SrV+ revealed a lectin-like fold that displays a putative preformed carbohydrate-binding site stabilized by a metal ion. Inhibition of this binding site may confer to humans a protection against dental caries and dissemination of the bacteria to extra-oral sites involved in life-threatening inflammatory diseases. This crystal structure constitutes a first step in understanding the structure-function relationship of antigens I/II and may help in delineating new preventive or therapeutic strategies against colonization of the host by oral streptococci.
==About this Structure==
==About this Structure==
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1JMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JMM OCA].
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1JMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMM OCA].
==Reference==
==Reference==
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[[Category: v-region]]
[[Category: v-region]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:22:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:18 2008''

Revision as of 11:24, 21 February 2008


1jmm, resolution 2.40Å

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Crystal structure of the V-region of Streptococcus mutans antigen I/II

Overview

Antigens I/II are large multifunctional adhesins from oral viridans streptococci that exert immunomodulatory effects on human cells and play important roles in inflammatory disorders. Among them, Streptococcus mutans plays a major role in the initiation of dental caries. The structure of the V-region (SrV+, residues 464-840) of the antigen I/II of S. mutans has been determined using the multiwavelength anomalous diffraction phasing technique with seleno-methionine-substituted recombinant protein and subsequently refined at 2.4 A resolution. The crystal structure of SrV+ revealed a lectin-like fold that displays a putative preformed carbohydrate-binding site stabilized by a metal ion. Inhibition of this binding site may confer to humans a protection against dental caries and dissemination of the bacteria to extra-oral sites involved in life-threatening inflammatory diseases. This crystal structure constitutes a first step in understanding the structure-function relationship of antigens I/II and may help in delineating new preventive or therapeutic strategies against colonization of the host by oral streptococci.

About this Structure

1JMM is a Single protein structure of sequence from Streptococcus mutans with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the V-region of Streptococcus mutans antigen I/II at 2.4 A resolution suggests a sugar preformed binding site., Troffer-Charlier N, Ogier J, Moras D, Cavarelli J, J Mol Biol. 2002 Apr 19;318(1):179-88. PMID:12054777

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