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[[Image:1jmm.jpg|left|200px]]
[[Image:1jmm.jpg|left|200px]]


{{Structure
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'''Crystal structure of the V-region of Streptococcus mutans antigen I/II'''
'''Crystal structure of the V-region of Streptococcus mutans antigen I/II'''
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[[Category: Ogier, J.]]
[[Category: Ogier, J.]]
[[Category: Troffer-Charlier, N.]]
[[Category: Troffer-Charlier, N.]]
[[Category: antigen i/ii]]
[[Category: Antigen i/ii]]
[[Category: v-region]]
[[Category: V-region]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:25:01 2008''
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Revision as of 18:25, 2 May 2008

File:1jmm.jpg

Template:STRUCTURE 1jmm

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. 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 Page seeded by OCA on Fri May 2 21:25:01 2008

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