2jdf
From Proteopedia
(New page: 200px<br /><applet load="2jdf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jdf, resolution 1.7Å" /> '''HUMAN GAMMA-B CRYSTAL...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The concept of novel binding proteins as an alternative to antibodies has | + | 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== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Affilin- | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17628592 17628592] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 21: | ||
[[Category: Rudolph, R.]] | [[Category: Rudolph, R.]] | ||
[[Category: Scheuermann, T.]] | [[Category: Scheuermann, T.]] | ||
| - | [[Category: Stubbs, M | + | [[Category: Stubbs, M T.]] |
[[Category: affilin]] | [[Category: affilin]] | ||
[[Category: artificial binding protein]] | [[Category: artificial binding protein]] | ||
| Line 31: | Line 31: | ||
[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:02:01 2008'' |
Revision as of 16:02, 21 February 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 Thu Feb 21 18:02:01 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
