2nuo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Crystal structures of complexes of an antiviral lectin griffithsin (GRFT), with glucose and N-acetylglucosamine were solved and refined at high, resolution. In both complexes, all six monosaccharide-binding sites of, GRFT were occupied and the mode of binding was similar to that of mannose., In our previous attempts to obtain a complex with N-acetylglucosamine by, soaking, only a single site was occupied; thus, cocrystallization was, clearly superior despite lower concentration of the ligand. Isothermal, titration calorimetric experiments with N-acetylglucosamine, glucose, and, mannose provided enthalpic evidence of distinct binding differences, between the three monosaccharides. A comparison of the mode of binding of, different monosaccharides is discussed in the context of the antiviral, activity of GRFT, based on specific binding to high-mannose-containing, complex carbohydrates found on viral envelopes.
+
Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes.
==About this Structure==
==About this Structure==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
-
[[Category: Ziolkowska, N.E.]]
+
[[Category: Ziolkowska, N E.]]
[[Category: EDO]]
[[Category: EDO]]
[[Category: GLC]]
[[Category: GLC]]
Line 26: Line 26:
[[Category: sugar binding protein]]
[[Category: sugar binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:16:48 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:16 2008''

Revision as of 16:11, 21 February 2008


2nuo, resolution 1.50Å

Drag the structure with the mouse to rotate

Crystal structure of a complex of griffithsin with glucose

Overview

Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes.

About this Structure

2NUO is a Single protein structure of sequence from Griffithsia with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine., Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A, Protein Sci. 2007 Jul;16(7):1485-9. Epub 2007 Jun 13. PMID:17567736

Page seeded by OCA on Thu Feb 21 18:11:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools