2jdg

From Proteopedia

Revision as of 11:49, 23 January 2008

AFFILIN BASED ON HUMAN GAMMA-B CRYSTALLIN

Overview

The concept of novel binding proteins as an alternative to antibodies has, undergone rapid development and is now ready for practical use in a wide, range of applications. Alternative binding proteins, based on suitable, scaffolds with desirable properties, are selected from combinatorial, libraries in vitro. Here, we describe an approach using a beta-sheet of, human gamma-B-crystallin to generate a universal binding site through, randomization of eight solvent-exposed amino acid residues selected, according to structural and sequence analyses. Specific variants, so-called Affilin, have been isolated from a phage display library against, a variety of targets that differ considerably in size and structure. The, isolated Affilin variants can be produced in Escherichia coli as soluble, proteins and have a high level of thermodynamic stability. The crystal, structures of the human wild-type gamma-B-crystallin and a selected, Affilin variant have been determined to 1.7 A and 2.0 A resolution, respectively. Comparison of the two molecules indicates that the human, gamma-B-crystallin tolerates amino acid exchanges with no major structural, change. We conclude that the intrinsically stable and easily expressed, gamma-B-crystallin provides a suitable framework for the generation of, novel binding molecules.

About this Structure

2JDG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Affilin-Novel Binding Molecules Based on Human gamma-B-Crystallin, an All beta-Sheet Protein., Ebersbach H, Fiedler E, Scheuermann T, Fiedler M, Stubbs MT, Reimann C, Proetzel G, Rudolph R, Fiedler U, J Mol Biol. 2007 Jun 22;. PMID:17628592

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