1rin: Difference between revisions

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New page: left|200px<br /><applet load="1rin" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rin, resolution 2.6Å" /> '''X-RAY CRYSTAL STRUCTU...
 
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[[Image:1rin.gif|left|200px]]<br /><applet load="1rin" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rin.gif|left|200px]]<br /><applet load="1rin" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rin, resolution 2.6&Aring;" />
caption="1rin, resolution 2.6&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION'''<br />
'''X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The x-ray crystal structure of pea lectin, in complex with a methyl, glycoside of the N-linked-type oligosaccharide trimannosyl core, methyl, 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, has been solved, by molecular replacement and refined at 2.6-A resolution. The R factor is, 0.183 for all data in the 8.0 to 2.6 A resolution range with an average, atomic temperature factor of 26.1 A2. Strong electron density for a single, mannose residue is found in the monosaccharide-binding site suggesting, that the trisaccharide binds primarily through one of the terminal, alpha-linked mannose residues. The complex is stabilized by hydrogen bonds, involving the protein residues Asp-81, Gly-99, Asn-125, Ala-217, and, Glu-218, and the carbohydrate oxygen atoms O3, O4, O5, and O6. In, addition, the carbohydrate makes van der Waals contacts with the protein, involving Phe-123 in particular. These interactions are very similar to, those found in the monosaccharide complexes with concanavalin A and, isolectin 1 of Lathyrus ochrus, confirming the structural relatedness of, this family of proteins. Comparison of the pea lectin complex with the, unliganded pea lectin and concanavalin A structures indicates differences, in the conformation and water structure of the unliganded binding sites of, these two proteins. Furthermore, a correlation between the position of the, carbohydrate oxygen atoms in the complex and the bound water molecules in, the unliganded binding sites is found. Binding of the trimannose core, through a single terminal monosaccharide residue strongly argues that an, additional fucose-binding site is responsible for the high affinity pea, lectin-oligosaccharide interactions.
The x-ray crystal structure of pea lectin, in complex with a methyl glycoside of the N-linked-type oligosaccharide trimannosyl core, methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, has been solved by molecular replacement and refined at 2.6-A resolution. The R factor is 0.183 for all data in the 8.0 to 2.6 A resolution range with an average atomic temperature factor of 26.1 A2. Strong electron density for a single mannose residue is found in the monosaccharide-binding site suggesting that the trisaccharide binds primarily through one of the terminal alpha-linked mannose residues. The complex is stabilized by hydrogen bonds involving the protein residues Asp-81, Gly-99, Asn-125, Ala-217, and Glu-218, and the carbohydrate oxygen atoms O3, O4, O5, and O6. In addition, the carbohydrate makes van der Waals contacts with the protein, involving Phe-123 in particular. These interactions are very similar to those found in the monosaccharide complexes with concanavalin A and isolectin 1 of Lathyrus ochrus, confirming the structural relatedness of this family of proteins. Comparison of the pea lectin complex with the unliganded pea lectin and concanavalin A structures indicates differences in the conformation and water structure of the unliganded binding sites of these two proteins. Furthermore, a correlation between the position of the carbohydrate oxygen atoms in the complex and the bound water molecules in the unliganded binding sites is found. Binding of the trimannose core through a single terminal monosaccharide residue strongly argues that an additional fucose-binding site is responsible for the high affinity pea lectin-oligosaccharide interactions.


==About this Structure==
==About this Structure==
1RIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with MAN, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RIN OCA].  
1RIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIN OCA].  


==Reference==
==Reference==
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Carver, J.P.]]
[[Category: Carver, J P.]]
[[Category: Einspahr, H.]]
[[Category: Einspahr, H.]]
[[Category: Hardman, K.D.]]
[[Category: Hardman, K D.]]
[[Category: Rini, J.M.]]
[[Category: Rini, J M.]]
[[Category: Suddath, F.L.]]
[[Category: Suddath, F L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MAN]]
[[Category: MAN]]
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[[Category: lectin]]
[[Category: lectin]]


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