We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hyq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hyq.gif|left|200px]]<br /><applet load="2hyq" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2hyq.gif|left|200px]]
-
caption="2hyq, resolution 2.00&Aring;" />
+
 
-
'''Crystal structure of a complex of griffithsin with 6alpha-mannobiose'''<br />
+
{{Structure
 +
|PDB= 2hyq |SIZE=350|CAPTION= <scene name='initialview01'>2hyq</scene>, resolution 2.00&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of a complex of griffithsin with 6alpha-mannobiose'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2HYQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Griffithsia Griffithsia] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYQ OCA].
+
2HYQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Griffithsia Griffithsia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYQ OCA].
==Reference==
==Reference==
-
Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin., Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A, Proteins. 2007 May 15;67(3):661-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17340634 17340634]
+
Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin., Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A, Proteins. 2007 May 15;67(3):661-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17340634 17340634]
[[Category: Griffithsia]]
[[Category: Griffithsia]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 19: Line 28:
[[Category: griffithsin]]
[[Category: griffithsin]]
[[Category: hiv]]
[[Category: hiv]]
-
[[Category: lectins]]
+
[[Category: lectin]]
[[Category: mannose binding]]
[[Category: mannose binding]]
-
[[Category: sars]]
+
[[Category: sar]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:11 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:23:17 2008''

Revision as of 15:23, 20 March 2008


PDB ID 2hyq

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a complex of griffithsin with 6alpha-mannobiose


Overview

The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X-ray crystallography, isothermal titration calorimetry, and molecular modeling. The structures of complexes of griffithsin with 1-->6alpha-mannobiose and with maltose were solved and refined at the resolution of 2.0 and 1.5 A, respectively. The thermodynamic parameters of binding of 1-->6alpha-mannobiose, maltose, and mannose to griffithsin were determined. Binding profiles of 1-->6alpha-mannobiose and mannose were similar with Kd values of 83.3 microM and 102 microM, respectively. The binding of maltose to griffithsin was significantly weaker, with a fourfold lower affinity (Kd = 394 microM). In all cases the binding at 30 degrees C was entropically rather than enthalpically driven. On the basis of the experimental crystal structures, as well as on previously determined structures of complexes with monosaccharides, it was possible to create a model of a tridentate complex of griffithsin with Man9GlcNAc2, a high mannose oligosaccharide commonly found on the surface of viral glycoproteins. All shorter oligomannoses could be modeled only as bidentate or monodentate complexes with griffithsin. The ability to mediate tight multivalent and multisite interactions with high-mannose oligosaccharides helps to explain the potent antiviral activity of griffithsin.

About this Structure

2HYQ is a Single protein structure of sequence from Griffithsia. Full crystallographic information is available from OCA.

Reference

Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin., Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A, Proteins. 2007 May 15;67(3):661-70. PMID:17340634

Page seeded by OCA on Thu Mar 20 17:23:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools