1cvn
From Proteopedia
(New page: 200px<br /><applet load="1cvn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvn, resolution 2.3Å" /> '''CONCANAVALIN A COMPLE...) |
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| - | [[Image:1cvn.gif|left|200px]]<br /><applet load="1cvn" size=" | + | [[Image:1cvn.gif|left|200px]]<br /><applet load="1cvn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cvn, resolution 2.3Å" /> | caption="1cvn, resolution 2.3Å" /> | ||
'''CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE'''<br /> | '''CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Despite the fact that complex saccharides play an important role in many | + | Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans. |
==About this Structure== | ==About this Structure== | ||
| - | 1CVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <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=1CVN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Naismith, J | + | [[Category: Naismith, J H.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: saccharide binding]] | [[Category: saccharide binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:12 2008'' |
Revision as of 10:10, 21 February 2008
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CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE
Overview
Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans.
About this Structure
1CVN is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of trimannoside recognition by concanavalin A., Naismith JH, Field RA, J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:8557713
Page seeded by OCA on Thu Feb 21 12:10:12 2008
