1wz1
From Proteopedia
(New page: 200px<br /> <applet load="1wz1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wz1, resolution 1.85Å" /> '''Crystal structure o...) |
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| - | [[Image:1wz1.gif|left|200px]]<br /> | + | [[Image:1wz1.gif|left|200px]]<br /><applet load="1wz1" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1wz1, resolution 1.85Å" /> | caption="1wz1, resolution 1.85Å" /> | ||
'''Crystal structure of the Fv fragment complexed with dansyl-lysine'''<br /> | '''Crystal structure of the Fv fragment complexed with dansyl-lysine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Antigen-induced structural changes in the Fv fragment of an anti-dansyl | + | Antigen-induced structural changes in the Fv fragment of an anti-dansyl immunoglobulin G were studied by X-ray crystallography and stopped-flow fluorescence measurement. The crystal structure of the Fv fragment complexed with dansyl-lysine was determined at a resolution of 1.85 A. The dansyl-lysine molecule bound to a narrow cavity formed by the complementarity-determining regions H3 and H1, the N-terminal region of the VH domain and L2 of the VL domain. The structure of the binding site in the crystal structure explained well the results of the previous nuclear magnetic resonance measurements. The hapten binding caused remarkable conformational changes in H3 and its environmental structures, including the hydration structure from those observed in the unliganded state. The tip of H3 moved about 12 A from its position in the unliganded state. In addition, because of the contacts of H3 with the VL domain at the domain interface, the conformational changes of H3 resulted in the relative rotation of the variable domains by 5 degrees from their association observed in the unliganded state. The hydrophobic interactions at the domain interface seemed to be particularly important for the mutual rotation of the domains. The stopped-flow fluorescence measurement monitoring the interaction of the dansyl group and the binding pocket revealed that H3 was in a conformational equilibrium of three consecutive conformational states in the presence of dansyl-lysine in solution; an unliganded state preventing the access of the hapten, another unliganded state able to bind the hapten and the complex. The conformational dynamics of H3 in recognizing and binding the hapten molecule are discussed on the basis of the structural information from the present and previous studies. |
==About this Structure== | ==About this Structure== | ||
| - | 1WZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with DNS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=DNS:'>DNS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: antigen-antibody fragent complex]] | [[Category: antigen-antibody fragent complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:35 2008'' |
Revision as of 13:49, 21 February 2008
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Crystal structure of the Fv fragment complexed with dansyl-lysine
Overview
Antigen-induced structural changes in the Fv fragment of an anti-dansyl immunoglobulin G were studied by X-ray crystallography and stopped-flow fluorescence measurement. The crystal structure of the Fv fragment complexed with dansyl-lysine was determined at a resolution of 1.85 A. The dansyl-lysine molecule bound to a narrow cavity formed by the complementarity-determining regions H3 and H1, the N-terminal region of the VH domain and L2 of the VL domain. The structure of the binding site in the crystal structure explained well the results of the previous nuclear magnetic resonance measurements. The hapten binding caused remarkable conformational changes in H3 and its environmental structures, including the hydration structure from those observed in the unliganded state. The tip of H3 moved about 12 A from its position in the unliganded state. In addition, because of the contacts of H3 with the VL domain at the domain interface, the conformational changes of H3 resulted in the relative rotation of the variable domains by 5 degrees from their association observed in the unliganded state. The hydrophobic interactions at the domain interface seemed to be particularly important for the mutual rotation of the domains. The stopped-flow fluorescence measurement monitoring the interaction of the dansyl group and the binding pocket revealed that H3 was in a conformational equilibrium of three consecutive conformational states in the presence of dansyl-lysine in solution; an unliganded state preventing the access of the hapten, another unliganded state able to bind the hapten and the complex. The conformational dynamics of H3 in recognizing and binding the hapten molecule are discussed on the basis of the structural information from the present and previous studies.
About this Structure
1WZ1 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Conformational dynamics of complementarity-determining region H3 of an anti-dansyl Fv fragment in the presence of its hapten., Nakasako M, Oka T, Mashumo M, Takahashi H, Shimada I, Yamaguchi Y, Kato K, Arata Y, J Mol Biol. 2005 Aug 19;351(3):627-40. PMID:16019026
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