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2jdf
From Proteopedia
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[[Image:2jdf.jpg|left|200px]] | [[Image:2jdf.jpg|left|200px]] | ||
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'''HUMAN GAMMA-B CRYSTALLIN''' | '''HUMAN GAMMA-B CRYSTALLIN''' | ||
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[[Category: Scheuermann, T.]] | [[Category: Scheuermann, T.]] | ||
[[Category: Stubbs, M T.]] | [[Category: Stubbs, M T.]] | ||
| - | [[Category: | + | [[Category: Affilin]] |
| - | [[Category: | + | [[Category: Artificial binding protein]] |
| - | [[Category: | + | [[Category: Eye lens protein]] |
| - | [[Category: | + | [[Category: Gamma crystallin]] |
| - | [[Category: | + | [[Category: Oxidation]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | [[Category: | + | [[Category: Polymorphism]] |
| - | [[Category: | + | [[Category: Structural protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:44:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:44, 4 May 2008
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
2JDF 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 Sep 7;372(1):172-85. Epub 2007 Jun 22. PMID:17628592 Page seeded by OCA on Sun May 4 08:44:04 2008
Categories: Homo sapiens | Single protein | Ebersbach, H. | Fiedler, E. | Fiedler, M. | Fiedler, U. | Proetzel, G. | Reimann, C. | Rudolph, R. | Scheuermann, T. | Stubbs, M T. | Affilin | Artificial binding protein | Eye lens protein | Gamma crystallin | Oxidation | Phosphorylation | Polymorphism | Structural protein
