1for: Difference between revisions

Revision as of 13:40, 21 February 2008

STRUCTURE DETERMINATION OF AN FAB FRAGMENT THAT NEUTRALIZES HUMAN RHINOVIRUS AND ANALYSIS OF THE FAB-VIRUS COMPLEX

OverviewOverview

The crystal structure of Fab17-IA, an antigen-binding fragment from a murine immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has been solved to 2.7 A resolution. Fab17-IA crystallized into three different space groups depending upon the method used to purify the intact antibody. The structure was determined by use of molecular and isomorphous replacement methods. The current model has a crystallographic R-factor of approximately 19% for 10,192 independent reflections between 8 and 2.7 A. Correlation coefficient calculations showed that the Fab17-IA structure can be fit into the Fab17-IA/HRV14 image reconstruction density to within 5 A positional accuracy and to within a few degrees of rotation. The resulting interface of the docked antibody was examined and showed extensive charge and shape complementarity with the virus surface that was supported by site-directed mutagenesis experiments. The success of this approach validates the utility of combining X-ray crystallography with cryo-electron microscopy of complex macromolecular assemblies.

About this StructureAbout this Structure

1FOR is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

ReferenceReference

Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex., Liu H, Smith TJ, Lee WM, Mosser AG, Rueckert RR, Olson NH, Cheng RH, Baker TS, J Mol Biol. 1994 Jul 8;240(2):127-37. PMID:8027997

Page seeded by OCA on Thu Feb 21 12:40:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1for.gif|left|200px]]<br />
+[[Image:1for.gif|left|200px]]<br /><applet load="1for" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1for" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1for, resolution 2.75&Aring;" />
 '''STRUCTURE DETERMINATION OF AN FAB FRAGMENT THAT NEUTRALIZES HUMAN RHINOVIRUS AND ANALYSIS OF THE FAB-VIRUS COMPLEX'''<br />
 ==Overview==
-The crystal structure of Fab17-IA, an antigen-binding fragment from a, murine immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has, been solved to 2.7 A resolution. Fab17-IA crystallized into three, different space groups depending upon the method used to purify the intact, antibody. The structure was determined by use of molecular and isomorphous, replacement methods. The current model has a crystallographic R-factor of, approximately 19% for 10,192 independent reflections between 8 and 2.7 A., Correlation coefficient calculations showed that the Fab17-IA structure, can be fit into the Fab17-IA/HRV14 image reconstruction density to within, 5 A positional accuracy and to within a few degrees of rotation. The, resulting interface of the docked antibody was examined and showed, extensive charge and shape complementarity with the virus surface that was, supported by site-directed mutagenesis experiments. The success of this, approach validates the utility of combining X-ray crystallography with, cryo-electron microscopy of complex macromolecular assemblies.
+The crystal structure of Fab17-IA, an antigen-binding fragment from a murine immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has been solved to 2.7 A resolution. Fab17-IA crystallized into three different space groups depending upon the method used to purify the intact antibody. The structure was determined by use of molecular and isomorphous replacement methods. The current model has a crystallographic R-factor of approximately 19% for 10,192 independent reflections between 8 and 2.7 A. Correlation coefficient calculations showed that the Fab17-IA structure can be fit into the Fab17-IA/HRV14 image reconstruction density to within 5 A positional accuracy and to within a few degrees of rotation. The resulting interface of the docked antibody was examined and showed extensive charge and shape complementarity with the virus surface that was supported by site-directed mutagenesis experiments. The success of this approach validates the utility of combining X-ray crystallography with cryo-electron microscopy of complex macromolecular assemblies.
 ==About this Structure==
-FOR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOR OCA].
+FOR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOR OCA].
 ==Reference==
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 [[Category: Protein complex]]
 [[Category: Liu, H.]]
-[[Category: Smith, T.J.]]
+[[Category: Smith, T J.]]
 [[Category: immunoglobulin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:30:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:55 2008''