We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1jfq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jfq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jfq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jfq| PDB=1jfq | SCENE= }}
{{STRUCTURE_1jfq| PDB=1jfq | SCENE= }}
-
'''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"===
-
==Overview==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_11673524}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[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

Image:1jfq.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jfq"
Personal tools