1fai
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fai OCA], [http://www.ebi.ac.uk/pdbsum/1fai PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fai RCSB]</span> | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:19:06 2008'' |
Revision as of 17:19, 30 March 2008
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| , resolution 2.7Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY
Overview
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.
About this Structure
1FAI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody., Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A, Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652
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