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1rin

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[[Image:1rin.gif|left|200px]]
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{{STRUCTURE_1rin| PDB=1rin | SCENE= }}
{{STRUCTURE_1rin| PDB=1rin | SCENE= }}
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'''X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION'''
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===X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8486683 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8486683}}
==About this Structure==
==About this Structure==
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[[Category: Suddath, F L.]]
[[Category: Suddath, F L.]]
[[Category: Lectin]]
[[Category: Lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:32:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:30:39 2008''

Revision as of 08:30, 28 July 2008

Image:1rin.png

Template:STRUCTURE 1rin

X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8486683

About this Structure

1RIN is a Protein complex structure of sequences from Pisum sativum. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution., Rini JM, Hardman KD, Einspahr H, Suddath FL, Carver JP, J Biol Chem. 1993 May 15;268(14):10126-32. PMID:8486683

Page seeded by OCA on Mon Jul 28 11:30:39 2008

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