2imm

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[[Image:2imm.gif|left|200px]]
[[Image:2imm.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2imm", creates the "Structure Box" on the page.
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{{STRUCTURE_2imm| PDB=2imm | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2imm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imm OCA], [http://www.ebi.ac.uk/pdbsum/2imm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2imm RCSB]</span>
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'''Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant'''
'''Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant'''
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[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Steipe, B.]]
[[Category: Steipe, B.]]
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[[Category: immunoglobulin]]
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[[Category: Immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:39:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:46:10 2008''
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Revision as of 04:39, 4 May 2008

Template:STRUCTURE 2imm

Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant


Overview

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

2IMM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 07:39:50 2008

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