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1qmo

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[[Image:1qmo.jpg|left|200px]]<br /><applet load="1qmo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qmo.jpg|left|200px]]
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caption="1qmo, resolution 3.5&Aring;" />
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'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION'''<br />
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{{Structure
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|PDB= 1qmo |SIZE=350|CAPTION= <scene name='initialview01'>1qmo</scene>, resolution 3.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QMO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lablab_purpureus Lablab purpureus] with <scene name='pdbligand=MAN:'>MAN</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=1QMO OCA].
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1QMO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lablab_purpureus Lablab purpureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMO OCA].
==Reference==
==Reference==
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The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL., Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L, J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10843844 10843844]
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The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL., Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L, J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10843844 10843844]
[[Category: Lablab purpureus]]
[[Category: Lablab purpureus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: sugar complex]]
[[Category: sugar complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:45 2008''

Revision as of 11:39, 20 March 2008

Image:1qmo.jpg


PDB ID 1qmo

Drag the structure with the mouse to rotate
, resolution 3.5Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF FRIL, A LEGUME LECTIN THAT DELAYS HEMATOPOIETIC PROGENITOR MATURATION


Overview

Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers.

About this Structure

1QMO is a Protein complex structure of sequences from Lablab purpureus. Full crystallographic information is available from OCA.

Reference

The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL., Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L, J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:10843844

Page seeded by OCA on Thu Mar 20 13:39:45 2008

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