3ax4
From Proteopedia
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ax4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ax4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ax4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ax4 PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ax4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ax4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ax4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ax4 PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lectins from Diocleinae subtribe belong to the family of legume lectins and are characterized by high identity between their amino acids sequences. It has been shown that punctual differences in amino acid sequences, such as one single amino acid or an alternative conformation, represent changes in biological activities caused by these lectins. Therefore, a more detailed understanding of three-dimensional structures of these proteins is essential for accurate analyzing the relationship between structure and function. In this study lectins purified from the seeds of Dioclea violacea (DVL) and Dioclea rostrata (DRL) were compared with regard to crystal structure and vasorelaxant properties. Differences in structure of lectins were found to be reflected in differences in vasorelaxant effects based on their high specificity and selectivity for cell glycans. Binding activity was related to the position of specific residues in the carbohydrate recognition domain (CRD). DVL complexed structure was solved by X-ray crystallography and was compared to native DVL and DRL. Therefore, DVL was co-crystallized with X-Man, and a molecular modeling with X-Man complexed with DVL was done to compare the complexed and native forms adjusted fit. The relatively narrow and deep CRD in DVL promotes little interaction with carbohydrates; in contrast, the wider and shallower CRD in DRL favors interaction. This seems to explain differences in the level of relaxation induced by DVL (43%) and DRL (96%) in rat aortic rings. | ||
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| + | Crystal structure of Dioclea violacea lectin and a comparative study of vasorelaxant properties with Dioclea rostrata lectin.,Bezerra MJ, Rodrigues NV, Pires Ade F, Bezerra GA, Nobre CB, Alencar KL, Soares PM, do Nascimento KS, Nagano CS, Martins JL, Gruber K, Sampaio AH, Delatorre P, Rocha BA, Assreuy AM, Cavada BS Int J Biochem Cell Biol. 2013 Apr;45(4):807-15. doi:, 10.1016/j.biocel.2013.01.012. Epub 2013 Jan 23. PMID:23353644<ref>PMID:23353644</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:57, 28 May 2014
Three-dimensional structure of lectin from Dioclea violacea and comparative vasorelaxant effects with Dioclea rostrata
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