2jdf: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1leu|1LEU]], [[1myv|1MYV]], [[1myx|1MYX]], [[1myy|1MYY]], [[1mz1|1MZ1]], [[1mz2|1MZ2]], [[1mz3|1MZ3]], [[2jdg|2JDG]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jdf OCA], [http://www.ebi.ac.uk/pdbsum/2jdf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jdf RCSB]</span>
}}
}}


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[[Category: structural protein]]
[[Category: structural protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:40:25 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:56:33 2008''

Revision as of 03:56, 31 March 2008

File:2jdf.jpg


PDB ID 2jdf

Drag the structure with the mouse to rotate
, resolution 1.7Å
Related: 1LEU, 1MYV, 1MYX, 1MYY, 1MZ1, 1MZ2, 1MZ3, 2JDG


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HUMAN GAMMA-B CRYSTALLIN


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

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