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.

1uac

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uac.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1uac.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uac| PDB=1uac | SCENE= }}
{{STRUCTURE_1uac| PDB=1uac | SCENE= }}
-
'''Crystal Structure of HYHEL-10 FV MUTANT SFSF Complexed with TURKEY WHITE LYSOZYME'''
+
===Crystal Structure of HYHEL-10 FV MUTANT SFSF Complexed with TURKEY WHITE LYSOZYME===
-
==Overview==
+
<!--
-
Decreased affinity of an antibody for a mutated epitope in an antigen can be enhanced and reversed by mutations in certain antibody residues. Here we describe the crystal structures of (a) the complex between a naturally mutated proteinaceous antigen and an antibody that was mutated and selected in vitro, and (b) the complex between the normal antigen and the mutated antibody. The mutated and selected antibody recognizes essentially the same epitope as in the wild-type antibody, indicating successful target site-directed functional alteration of the antibody. In comparing the structure of the mutated antigen-mutant antibody complex with the previously established structure of the wild-type antigen-wild-type antibody complex, we found that the enhanced affinity of the mutated antibody for the mutant antigen originated not from improvements in local complementarity around the mutated sites but from subtle and critical structural changes in nonmutated sites, including an increase in variable domain interactions. Our findings indicate that only a few mutations in the antigen-binding region of an antibody can lead to some structural changes in its paratopes, emphasizing the critical roles of the plasticity of loops in the complementarity-determining region and also the importance of the plasticity of the interaction between the variable regions of immunoglobulin heavy and light chains in determining the specificity of an antibody.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12709438}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12709438 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12709438}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hyhel-10]]
[[Category: Hyhel-10]]
[[Category: Mutant]]
[[Category: Mutant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:57:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:26:05 2008''

Revision as of 13:26, 27 July 2008

Image:1uac.png

Template:STRUCTURE 1uac

Crystal Structure of HYHEL-10 FV MUTANT SFSF Complexed with TURKEY WHITE LYSOZYME

Template:ABSTRACT PUBMED 12709438

About this Structure

1UAC is a Protein complex structure of sequences from Meleagris gallopavo and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10., Kumagai I, Nishimiya Y, Kondo H, Tsumoto K, J Biol Chem. 2003 Jul 4;278(27):24929-36. Epub 2003 Apr 22. PMID:12709438

Page seeded by OCA on Sun Jul 27 16:26:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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