1g8w

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(New page: 200px<br /><applet load="1g8w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g8w, resolution 2.8&Aring;" /> '''IMPROVED STRUCTURE OF...)
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[[Image:1g8w.gif|left|200px]]<br /><applet load="1g8w" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1g8w, resolution 2.8&Aring;" />
'''IMPROVED STRUCTURE OF PHYTOHEMAGGLUTININ-L FROM THE KIDNEY BEAN'''<br />
'''IMPROVED STRUCTURE OF PHYTOHEMAGGLUTININ-L FROM THE KIDNEY BEAN'''<br />
==Overview==
==Overview==
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The legume lectins are widely used as a model system for studying, protein-carbohydrate and protein-protein interactions. They exhibit a, fascinating quaternary structure variation, which becomes important when, they interact with multivalent glycoconjugates, for instance those on cell, surfaces. Recently, it has become clear that certain lectins form weakly, associated oligomers. This phenomenon may play a role in the regulation of, receptor crosslinking and subsequent signal transduction. The crystal, structure of DB58, a dimeric lectin from the legume Dolichos biflorus, reveals a separate dimer of a previously unobserved type, in addition to a, tetramer consisting of two such dimers. This tetramer resembles that, formed by DBL, the seed lectin from the same plant. A single amino acid, substitution in DB58 affects the conformation and flexibility of a loop in, the canonical dimer interface. This disrupts the formation of a stable, DBL-like tetramer in solution, but does not prohibit its formation in, suitable conditions, which greatly increases the possibilities for the, cross-linking of multivalent ligands. The non-canonical DB58 dimer has a, buried symmetrical alpha helix, which can be present in the crystal in, either of two antiparallel orientations. Two existing structures and, datasets for lectins with similar quaternary structures were reconsidered., A central alpha helix could be observed in the soybean lectin, but not in, the leucoagglutinating lectin from Phaseolus vulgaris. The relative, position and orientation of the carbohydrate-binding sites in the DB58, dimer may affect its ability to crosslink mulitivalent ligands, compared, to the other legume lectin dimers.
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The legume lectins are widely used as a model system for studying protein-carbohydrate and protein-protein interactions. They exhibit a fascinating quaternary structure variation, which becomes important when they interact with multivalent glycoconjugates, for instance those on cell surfaces. Recently, it has become clear that certain lectins form weakly associated oligomers. This phenomenon may play a role in the regulation of receptor crosslinking and subsequent signal transduction. The crystal structure of DB58, a dimeric lectin from the legume Dolichos biflorus reveals a separate dimer of a previously unobserved type, in addition to a tetramer consisting of two such dimers. This tetramer resembles that formed by DBL, the seed lectin from the same plant. A single amino acid substitution in DB58 affects the conformation and flexibility of a loop in the canonical dimer interface. This disrupts the formation of a stable DBL-like tetramer in solution, but does not prohibit its formation in suitable conditions, which greatly increases the possibilities for the cross-linking of multivalent ligands. The non-canonical DB58 dimer has a buried symmetrical alpha helix, which can be present in the crystal in either of two antiparallel orientations. Two existing structures and datasets for lectins with similar quaternary structures were reconsidered. A central alpha helix could be observed in the soybean lectin, but not in the leucoagglutinating lectin from Phaseolus vulgaris. The relative position and orientation of the carbohydrate-binding sites in the DB58 dimer may affect its ability to crosslink mulitivalent ligands, compared to the other legume lectin dimers.
==About this Structure==
==About this Structure==
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1G8W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] with NAG, 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=1G8W OCA].
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1G8W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] with <scene name='pdbligand=NAG:'>NAG</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=1G8W OCA].
==Reference==
==Reference==
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[[Category: Buts, L.]]
[[Category: Buts, L.]]
[[Category: Dao-Thi, M.]]
[[Category: Dao-Thi, M.]]
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[[Category: Etzler, M.E.]]
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[[Category: Etzler, M E.]]
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[[Category: Hamelryck, T.W.]]
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[[Category: Hamelryck, T W.]]
[[Category: Loris, R.]]
[[Category: Loris, R.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
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[[Category: legume lectin]]
[[Category: legume lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:49:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:26 2008''

Revision as of 10:47, 21 February 2008

Image:1g8w.gif

1g8w, resolution 2.8Å

Drag the structure with the mouse to rotate

IMPROVED STRUCTURE OF PHYTOHEMAGGLUTININ-L FROM THE KIDNEY BEAN

Overview

The legume lectins are widely used as a model system for studying protein-carbohydrate and protein-protein interactions. They exhibit a fascinating quaternary structure variation, which becomes important when they interact with multivalent glycoconjugates, for instance those on cell surfaces. Recently, it has become clear that certain lectins form weakly associated oligomers. This phenomenon may play a role in the regulation of receptor crosslinking and subsequent signal transduction. The crystal structure of DB58, a dimeric lectin from the legume Dolichos biflorus reveals a separate dimer of a previously unobserved type, in addition to a tetramer consisting of two such dimers. This tetramer resembles that formed by DBL, the seed lectin from the same plant. A single amino acid substitution in DB58 affects the conformation and flexibility of a loop in the canonical dimer interface. This disrupts the formation of a stable DBL-like tetramer in solution, but does not prohibit its formation in suitable conditions, which greatly increases the possibilities for the cross-linking of multivalent ligands. The non-canonical DB58 dimer has a buried symmetrical alpha helix, which can be present in the crystal in either of two antiparallel orientations. Two existing structures and datasets for lectins with similar quaternary structures were reconsidered. A central alpha helix could be observed in the soybean lectin, but not in the leucoagglutinating lectin from Phaseolus vulgaris. The relative position and orientation of the carbohydrate-binding sites in the DB58 dimer may affect its ability to crosslink mulitivalent ligands, compared to the other legume lectin dimers.

About this Structure

1G8W is a Single protein structure of sequence from Phaseolus vulgaris with , and as ligands. Full crystallographic information is available from OCA.

Reference

Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus., Buts L, Dao-Thi MH, Loris R, Wyns L, Etzler M, Hamelryck T, J Mol Biol. 2001 May 25;309(1):193-201. PMID:11491289

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