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| | {{STRUCTURE_1jfq| PDB=1jfq | SCENE= }} | | {{STRUCTURE_1jfq| PDB=1jfq | SCENE= }} |
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| - | '''ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBODY 36-71, "FAB 36-71"'''
| + | ===ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBODY 36-71, "FAB 36-71"=== |
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| - | ==Overview==
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| - | Alanine scanning was used to determine the affinity contributions of 10 side chain amino acids (residues at position 50-60 inclusive) of H chain complementarity-determining region 2 (HCDR2) of the somatically mutated high-affinity anti-p-azophenylarsonate Ab, 36-71. Each mutated H chain gene was expressed in the context of mutated (36-71L) and the unmutated (36-65L) L chains to also assess the contribution of L chain mutations to affinity. Combined data from fluorescence quenching, direct binding, inhibition, and capture assays indicated that mutating H:Tyr(50) and H:Tyr(57) to Ala in the 36-71 H chain results in significant loss of binding with both mutated (36-71L) or unmutated (36-65L) L chain, although the decrease was more pronounced when unmutated L chain was used. All other HCDR2 mutations in 36-71 had minimal effect on Ab affinity when expressed with 36-71 L chain. However, in the context of unmutated L chain, of H:Gly(54) to Ala resulted in significant loss of binding, while Abs containing Asn(52) to Ala, Pro(53) to Ala, or Ile(58) to Ala mutation exhibited 4.3- to 7.1-fold reduced affinities. When alanine scanning was performed instead on certain HCDR2 residues of the germline-encoded (unmutated) 36-65 Ab and expressed with unmutated L chain as Fab in bacteria, these mutants exhibited affinities similar to or slightly higher than the wild-type 36-65. These findings indicate an important role of certain HCDR2 side chain residues on Ab affinity and the constraints imposed by L chain mutations in maintaining Ag binding.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11673524}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11673524 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11673524}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Viswanathan, M.]] | | [[Category: Viswanathan, M.]] |
| | [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:10:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:10:44 2008'' |
Revision as of 17:10, 1 July 2008
Template:STRUCTURE 1jfq
ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBODY 36-71, "FAB 36-71"
Template:ABSTRACT PUBMED 11673524
About this Structure
1JFQ is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural analysis of mutants of high-affinity and low-affinity p-azophenylarsonate-specific antibodies generated by alanine scanning of heavy chain complementarity-determining region 2., Parhami-Seren B, Viswanathan M, Strong RK, Margolies MN, J Immunol. 2001 Nov 1;167(9):5129-35. PMID:11673524
Page seeded by OCA on Tue Jul 1 20:10:44 2008
