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''' | + | {{Structure |
| + | |PDB= 2jdf |SIZE=350|CAPTION= <scene name='initialview01'>2jdf</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN GAMMA-B CRYSTALLIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JDF is a [ | + | 2JDF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JDF OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/17628592 17628592] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:40:25 2008'' |
Revision as of 15:40, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 17:40:25 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
