1iiy
From Proteopedia
(New page: 200px<br /> <applet load="1iiy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iiy" /> '''SOLUTION NMR STRUCTURE OF COMPLEX OF 1:2 CY...) |
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'''SOLUTION NMR STRUCTURE OF COMPLEX OF 1:2 CYANOVIRIN-N:MAN-ALPHA1,2-MAN-ALPHA RESTRAINED REGULARIZED MEAN COORDINATES'''<br /> | '''SOLUTION NMR STRUCTURE OF COMPLEX OF 1:2 CYANOVIRIN-N:MAN-ALPHA1,2-MAN-ALPHA RESTRAINED REGULARIZED MEAN COORDINATES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Cyanovirin-N (CVN) is a novel, 11 kDa cyanobacterial protein | + | BACKGROUND: Cyanovirin-N (CVN) is a novel, 11 kDa cyanobacterial protein that potently inhibits viral entry by diverse strains of HIV through high-affinity carbohydrate-mediated interactions with the viral envelope glycoprotein gp120. CVN contains two symmetry-related carbohydrate binding sites of differing affinities that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinities, the carbohydrates that also mediate CVN:gp120 binding. High-resolution structural studies of CVN in complex with a representative oligosaccharide are desirable for understanding the structural basis for this unprecedented specificity. RESULTS: We have determined by multidimensional heteronuclear NMR spectroscopy the three-dimensional solution structure of CVN in complex with two equivalents of the disaccharide Manalpha1-2Manalpha, a high-affinity ligand which represents the terminal-accessible disaccharide present in Man(8) D1D3 and Man(9). The structure reveals that the bound disaccharide adopts the stacked conformation, thereby explaining the selectivity for Man(8) D1D3 and Man(9) over other oligomannose structures, and presents two novel carbohydrate binding sites that account for the differing affinities of the two sites. The high-affinity site comprises a deep pocket that nearly envelops the disaccharide, while the lower-affinity site comprises a semicircular cleft that partially surrounds the disaccharide. The approximately 40 A spacing of the two binding sites provides a simple model for CVN:gp120 binding. CONCLUSIONS: The CVN:Manalpha1-2Manalpha complex provides the first high-resolution structure of a mannose-specific protein-carbohydrate complex with nanomolar affinity and presents a new carbohydrate binding motif, as well as a new class of carbohydrate binding protein, that facilitates divalent binding via a monomeric protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1IIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http:// | + | 1IIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nostoc ellipsosporum]] | [[Category: Nostoc ellipsosporum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bewley, C | + | [[Category: Bewley, C A.]] |
[[Category: 2-man-alpha]] | [[Category: 2-man-alpha]] | ||
[[Category: hiv-inactivating protein]] | [[Category: hiv-inactivating protein]] | ||
[[Category: man-alpha1]] | [[Category: man-alpha1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:18 2008'' |
Revision as of 11:12, 21 February 2008
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SOLUTION NMR STRUCTURE OF COMPLEX OF 1:2 CYANOVIRIN-N:MAN-ALPHA1,2-MAN-ALPHA RESTRAINED REGULARIZED MEAN COORDINATES
Overview
BACKGROUND: Cyanovirin-N (CVN) is a novel, 11 kDa cyanobacterial protein that potently inhibits viral entry by diverse strains of HIV through high-affinity carbohydrate-mediated interactions with the viral envelope glycoprotein gp120. CVN contains two symmetry-related carbohydrate binding sites of differing affinities that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinities, the carbohydrates that also mediate CVN:gp120 binding. High-resolution structural studies of CVN in complex with a representative oligosaccharide are desirable for understanding the structural basis for this unprecedented specificity. RESULTS: We have determined by multidimensional heteronuclear NMR spectroscopy the three-dimensional solution structure of CVN in complex with two equivalents of the disaccharide Manalpha1-2Manalpha, a high-affinity ligand which represents the terminal-accessible disaccharide present in Man(8) D1D3 and Man(9). The structure reveals that the bound disaccharide adopts the stacked conformation, thereby explaining the selectivity for Man(8) D1D3 and Man(9) over other oligomannose structures, and presents two novel carbohydrate binding sites that account for the differing affinities of the two sites. The high-affinity site comprises a deep pocket that nearly envelops the disaccharide, while the lower-affinity site comprises a semicircular cleft that partially surrounds the disaccharide. The approximately 40 A spacing of the two binding sites provides a simple model for CVN:gp120 binding. CONCLUSIONS: The CVN:Manalpha1-2Manalpha complex provides the first high-resolution structure of a mannose-specific protein-carbohydrate complex with nanomolar affinity and presents a new carbohydrate binding motif, as well as a new class of carbohydrate binding protein, that facilitates divalent binding via a monomeric protein.
About this Structure
1IIY is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Solution structure of a cyanovirin-N:Man alpha 1-2Man alpha complex: structural basis for high-affinity carbohydrate-mediated binding to gp120., Bewley CA, Structure. 2001 Oct;9(10):931-40. PMID:11591348
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