This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1jpt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jpt.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jpt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jpt| PDB=1jpt | SCENE= }}
{{STRUCTURE_1jpt| PDB=1jpt | SCENE= }}
-
'''Crystal Structure of Fab D3H44'''
+
===Crystal Structure of Fab D3H44===
-
==Overview==
+
<!--
-
The outstanding importance of the antigen-antibody recognition process for the survival and defence strategy of higher organisms is in sharp contrast to the limited high resolution structural data available on antibody-antigen pairs with antigenic proteins. The limitation is the most severe for structural data not restricted to the antigen-antibody complex but extending to the uncomplexed antigen and antibody. We report the crystal structure of the complex between tissue factor (TF) and the humanized Fab fragment D3h44 at a resolution of 1.85 A together with the structure of uncomplexed D3h44 at the same resolution. In conjunction with the previously reported 1.7 A crystal structure of uncomplexed TF, a unique opportunity is generated to explore details of the recognition process. The TF.D3h44 interface is characterised by a high number of polar interactions, including as may as 46 solvent molecules. Conformational changes upon complex formation are very small and almost exclusively limited to the reorientation of side-chains. The binding epitope is in complete agreement with earlier mutagenesis experiments. A revaluation of two other antibody-antigen pairs reported at similar resolutions, shows that all these complexes are very similar with respect to the solvation of the interface, the number of solvent positions conserved in the uncomplexed and complexed proteins and the number of water molecules expelled from the surface and replaced by hydrophilic atoms from the binding partner upon complex formation. A strategy is proposed on how to exploit this high resolution structural data to guide the affinity maturation of humanised antibodies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11601848}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11601848 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11601848}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Crystal structure]]
[[Category: Crystal structure]]
[[Category: Humanized antibody]]
[[Category: Humanized antibody]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:34:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:36:44 2008''

Revision as of 17:36, 1 July 2008

Image:1jpt.png

Template:STRUCTURE 1jpt

Crystal Structure of Fab D3H44

Template:ABSTRACT PUBMED 11601848

About this Structure

Full crystallographic information is available from OCA.

Reference

The 1.85 A resolution crystal structures of tissue factor in complex with humanized Fab D3h44 and of free humanized Fab D3h44: revisiting the solvation of antigen combining sites., Faelber K, Kirchhofer D, Presta L, Kelley RF, Muller YA, J Mol Biol. 2001 Oct 12;313(1):83-97. PMID:11601848

Page seeded by OCA on Tue Jul 1 20:36:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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