2JDF
Human gamma-B crystallin
Summary for 2JDF
| Entry DOI | 10.2210/pdb2jdf/pdb |
| Related | 1LEU 1MYV 1MYX 1MYY 1MZ1 1MZ2 1MZ3 2JDG |
| Descriptor | GAMMA CRYSTALLIN B (2 entities in total) |
| Functional Keywords | artificial binding protein, structural protein, eye lens protein, gamma crystallin, affilin, oxidation, polymorphism, phosphorylation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 21873.63 |
| Authors | Ebersbach, H.,Fiedler, E.,Scheuermann, T.,Fiedler, M.,Stubbs, M.T.,Reimann, C.,Proetzel, G.,Rudolph, R.,Fiedler, U. (deposition date: 2007-01-08, release date: 2007-07-24, Last modification date: 2024-05-08) |
| Primary citation | Ebersbach, H.,Fiedler, E.,Scheuermann, T.,Fiedler, M.,Stubbs, M.T.,Reimann, C.,Proetzel, G.,Rudolph, R.,Fiedler, U. Affilin-Novel Binding Molecules Based on Human Gamma-B-Crystallin, an All Beta-Sheet Protein. J.Mol.Biol., 372:172-, 2007 Cited by PubMed Abstract: 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. PubMed: 17628592DOI: 10.1016/J.JMB.2007.06.045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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