This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


8fab

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:8fab.gif|left|200px]]<br /><applet load="8fab" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:8fab.gif|left|200px]]
-
caption="8fab, resolution 1.8&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION'''<br />
+
{{Structure
 +
|PDB= 8fab |SIZE=350|CAPTION= <scene name='initialview01'>8fab</scene>, resolution 1.8&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
8FAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAB OCA].
+
8FAB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAB OCA].
==Reference==
==Reference==
-
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten., Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN, Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2015229 2015229]
+
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten., Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN, Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2015229 2015229]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 17: Line 26:
[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:17:54 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:15:25 2008''

Revision as of 17:15, 20 March 2008


PDB ID 8fab

Drag the structure with the mouse to rotate
, resolution 1.8Å
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION


Overview

The structure of the antigen-binding fragment (Fab) of an anti-p-azophenylarsonate monoclonal antibody, 36-71, bearing a major cross-reactive idiotype of A/J mice has been refined to an R factor of 24.8% at a resolution of 1.85 A. The previously solved partial structure of this Fab at a resolution of 2.9 A (Rose et al., 1990) was used as an initial model for refinement against the high-resolution data. The complex with hapten has been modeled by docking the small-molecule crystal structure of phenylarsonic acid into the structure of the native Fab on the basis of a low-resolution electron density map of the complex. In this model, residue Arg-96 in the light chain and residues Asn-35, Trp-47, and Ser-99 in the heavy chain contact the arsonate moiety of the hapten; an additional bond is found between the arsonate group and a tightly bound water molecule. The phenyl moiety of the hapten packs against two tyrosine side chains at positions 50 and 106 in the heavy chain. Residue Arg-96 in the light chain had been implicated as involved in hapten binding on the basis of previous experiments, and indeed, this residue appears to play a crucial role in this model. Experiments employing site-directed mutagenesis directly support this conclusion. The heavy-chain complementarity-determining regions have novel conformations not previously observed in immunoglobulins except for the recently solved anti-p-azophenylarsonate Fab R 19.9 (Lascombe et al., 1989).

About this Structure

8FAB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten., Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN, Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:2015229

Page seeded by OCA on Thu Mar 20 19:15:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools