1svx
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= MALE, B4034, Z5632, ECS5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= MALE, B4034, Z5632, ECS5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mj0|1MJ0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svx OCA], [http://www.ebi.ac.uk/pdbsum/1svx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svx RCSB]</span> | ||
}} | }} | ||
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[[Category: selected binder]] | [[Category: selected binder]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:39 2008'' |
Revision as of 20:47, 30 March 2008
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| , resolution 2.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | MALE, B4034, Z5632, ECS5017 (Escherichia coli) | ||||||
| Related: | 1MJ0
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein
Overview
We report here the evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding. Using a consensus design strategy, we generated combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces. Libraries of two and three repeats, flanked by 'capping repeats,' were used in ribosome-display selections against maltose binding protein (MBP) and two eukaryotic kinases. We rapidly enriched target-specific binders with affinities in the low nanomolar range and determined the crystal structure of one of the selected AR proteins in complex with MBP at 2.3 A resolution. The interaction relies on the randomized positions of the designed AR protein and is comparable to natural, heterodimeric protein-protein interactions. Thus, our AR protein libraries are valuable sources for binding molecules and, because of the very favorable biophysical properties of the designed AR proteins, an attractive alternative to antibody libraries.
About this Structure
1SVX is a Protein complex structure of sequences from [1] and Escherichia coli. Full crystallographic information is available from OCA.
Reference
High-affinity binders selected from designed ankyrin repeat protein libraries., Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, Grutter MG, Pluckthun A, Nat Biotechnol. 2004 May;22(5):575-82. Epub 2004 Apr 18. PMID:15097997 [[Category: ]]
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