2imn: Difference between revisions
New page: left|200px<br /><applet load="2imn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2imn, resolution 1.97Å" /> '''Refined crystal stru... |
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==Overview== | ==Overview== | ||
We report the solution of the crystal structure of a mutant of the | We report the solution of the crystal structure of a mutant of the immunoglobulin VL domain of the antibody McPC603, in which the complementarity-determining region 1 segment is replaced with that of a different antibody. The wild-type and mutant crystal structures have been refined to a crystallographic R-factor of 14.9% at a nominal resolution of 1.97 A. A detailed description of the structures is given. Crystal packing results in a dimeric association of domains, in a fashion closely resembling that of an Fv fragment. The comparison of this VL domain with the same domain in the Fab fragment of McPC603 shows that the structure of an immunoglobulin VL domain is largely independent of its mode of association, even in places where the inter-subunit contacts are not conserved between VL and VH. In all three complementarity-determining regions we observe conformations that would not have been predicted by the canonical structure hypothesis. Significant differences between the VL domain dimer and the Fab fragment in the third complementarity-determining region show that knowledge of the structure of the dimerization partner and its exact mode of association may be needed to predict the precise conformation of antigen-binding loops. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: imunoglobulin]] | [[Category: imunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:11 2008'' | ||
Revision as of 18:54, 21 February 2008
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Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
OverviewOverview
We report the solution of the crystal structure of a mutant of the immunoglobulin VL domain of the antibody McPC603, in which the complementarity-determining region 1 segment is replaced with that of a different antibody. The wild-type and mutant crystal structures have been refined to a crystallographic R-factor of 14.9% at a nominal resolution of 1.97 A. A detailed description of the structures is given. Crystal packing results in a dimeric association of domains, in a fashion closely resembling that of an Fv fragment. The comparison of this VL domain with the same domain in the Fab fragment of McPC603 shows that the structure of an immunoglobulin VL domain is largely independent of its mode of association, even in places where the inter-subunit contacts are not conserved between VL and VH. In all three complementarity-determining regions we observe conformations that would not have been predicted by the canonical structure hypothesis. Significant differences between the VL domain dimer and the Fab fragment in the third complementarity-determining region show that knowledge of the structure of the dimerization partner and its exact mode of association may be needed to predict the precise conformation of antigen-binding loops.
About this StructureAbout this Structure
2IMN is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant., Steipe B, Pluckthun A, Huber R, J Mol Biol. 1992 Jun 5;225(3):739-53. PMID:1602480
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