1mvq
From Proteopedia
(New page: 200px<br /><applet load="1mvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mvq, resolution 1.77Å" /> '''Cratylia mollis lect...) |
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| - | [[Image:1mvq.gif|left|200px]]<br /><applet load="1mvq" size=" | + | [[Image:1mvq.gif|left|200px]]<br /><applet load="1mvq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mvq, resolution 1.77Å" /> | caption="1mvq, resolution 1.77Å" /> | ||
'''Cratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannose'''<br /> | '''Cratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carbohydrate-protein interactions play a key role in many biological | + | Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein binding profiles. We report the primary structure of Cramoll, determined by Edman degradation and mass spectrometry and its 1.77 A crystallographic structure and compare it with the three-dimensional structure of Con A in an attempt to understand how differential binding can be achieved by similar or nearly identical structures. We report here that Cramoll consists of 236 residues, with 82% identity with Con A, and that its topological architecture is essentially identical to Con A, because the Calpha positional differences are below 3.5 A. Cramoll and Con A have identical binding sites for MealphaMan, Mn2+, and Ca2+. However, we observed six substitutions in a groove adjacent to the extended binding site and two in the extended binding site that may explain the differences in binding of oligosaccharides and glycoproteins between Cramoll and Con A. |
==About this Structure== | ==About this Structure== | ||
| - | 1MVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cratylia_mollis Cratylia mollis] with MMA, CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cratylia_mollis Cratylia mollis] with <scene name='pdbligand=MMA:'>MMA</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cratylia mollis]] | [[Category: Cratylia mollis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Coelho, L | + | [[Category: Coelho, L C.]] |
| - | [[Category: Correia, M | + | [[Category: Correia, M T.]] |
| - | [[Category: Greene, L | + | [[Category: Greene, L J.]] |
[[Category: Oliva, G.]] | [[Category: Oliva, G.]] | ||
| - | [[Category: Oliveira, P | + | [[Category: Oliveira, P S.]] |
| - | [[Category: Souza, G | + | [[Category: Souza, G A.de.]] |
[[Category: Trapani, S.]] | [[Category: Trapani, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: legume lectin]] | [[Category: legume lectin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:30 2008'' |
Revision as of 11:59, 21 February 2008
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Cratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannose
Overview
Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein binding profiles. We report the primary structure of Cramoll, determined by Edman degradation and mass spectrometry and its 1.77 A crystallographic structure and compare it with the three-dimensional structure of Con A in an attempt to understand how differential binding can be achieved by similar or nearly identical structures. We report here that Cramoll consists of 236 residues, with 82% identity with Con A, and that its topological architecture is essentially identical to Con A, because the Calpha positional differences are below 3.5 A. Cramoll and Con A have identical binding sites for MealphaMan, Mn2+, and Ca2+. However, we observed six substitutions in a groove adjacent to the extended binding site and two in the extended binding site that may explain the differences in binding of oligosaccharides and glycoproteins between Cramoll and Con A.
About this Structure
1MVQ is a Single protein structure of sequence from Cratylia mollis with , and as ligands. Full crystallographic information is available from OCA.
Reference
Amino acid sequence and tertiary structure of Cratylia mollis seed lectin., De Souza GA, Oliveira PS, Trapani S, Santos AC, Rosa JC, Laure HJ, Faca VM, Correia MT, Tavares GA, Oliva G, Coelho LC, Greene LJ, Glycobiology. 2003 Dec;13(12):961-72. Epub 2003 Sep 9. PMID:12966038
Page seeded by OCA on Thu Feb 21 13:59:30 2008
Categories: Cratylia mollis | Single protein | Coelho, L C. | Correia, M T. | Greene, L J. | Oliva, G. | Oliveira, P S. | Souza, G A.de. | Trapani, S. | CA | MMA | MN | Legume lectin
