2fgw
From Proteopedia
(New page: 200px<br /> <applet load="2fgw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fgw, resolution 3.0Å" /> '''X-RAY STRUCTURES OF ...) |
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| - | [[Image:2fgw.gif|left|200px]]<br /> | + | [[Image:2fgw.gif|left|200px]]<br /><applet load="2fgw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2fgw" size=" | + | |
caption="2fgw, resolution 3.0Å" /> | caption="2fgw, resolution 3.0Å" /> | ||
'''X-RAY STRUCTURES OF FRAGMENTS FROM BINDING AND NONBINDING VERSIONS OF A HUMANIZED ANTI-CD18 ANTIBODY: STRUCTURAL INDICATIONS OF THE KEY ROLE OF VH RESIDUES 59 TO 65'''<br /> | '''X-RAY STRUCTURES OF FRAGMENTS FROM BINDING AND NONBINDING VERSIONS OF A HUMANIZED ANTI-CD18 ANTIBODY: STRUCTURAL INDICATIONS OF THE KEY ROLE OF VH RESIDUES 59 TO 65'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray crystal structures of fragments from two different humanized | + | X-ray crystal structures of fragments from two different humanized anti-CD18 antibodies are reported. The Fv fragment of the nonbinding version has been refined in space group C2 with a = 64.2 A, b = 61.3 A, c = 51.8 A, and beta = 99 degrees to an R-value of 18.0% at 1.9 A, and the Fab fragment of the tight-binding version has been refined in space group P3 with a = 101. A and c = 45.5 A to an R-value of 17.8% at 3.0 A resolution. The very large difference in their binding affinity (> 1000-fold) is attributed to large and local structural differences in the C-terminal part of CDR-H2, and from this we conclude there is direct contact between this region and antigen when they combine. X-ray structures of antibody-antigen complexes available in the literature have yet to show this part of CDR-H2 in contact with antigen, despite its hypervariable sequence. Implications of this result for antibody humanization are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 2FGW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 2FGW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:13 2008'' |
Revision as of 15:21, 21 February 2008
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X-RAY STRUCTURES OF FRAGMENTS FROM BINDING AND NONBINDING VERSIONS OF A HUMANIZED ANTI-CD18 ANTIBODY: STRUCTURAL INDICATIONS OF THE KEY ROLE OF VH RESIDUES 59 TO 65
Overview
X-ray crystal structures of fragments from two different humanized anti-CD18 antibodies are reported. The Fv fragment of the nonbinding version has been refined in space group C2 with a = 64.2 A, b = 61.3 A, c = 51.8 A, and beta = 99 degrees to an R-value of 18.0% at 1.9 A, and the Fab fragment of the tight-binding version has been refined in space group P3 with a = 101. A and c = 45.5 A to an R-value of 17.8% at 3.0 A resolution. The very large difference in their binding affinity (> 1000-fold) is attributed to large and local structural differences in the C-terminal part of CDR-H2, and from this we conclude there is direct contact between this region and antigen when they combine. X-ray structures of antibody-antigen complexes available in the literature have yet to show this part of CDR-H2 in contact with antigen, despite its hypervariable sequence. Implications of this result for antibody humanization are discussed.
About this Structure
2FGW is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: structural indications of the key role of VH residues 59 to 65., Eigenbrot C, Gonzalez T, Mayeda J, Carter P, Werther W, Hotaling T, Fox J, Kessler J, Proteins. 1994 Jan;18(1):49-62. PMID:7908437
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