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1svx

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{{STRUCTURE_1svx| PDB=1svx | SCENE= }}
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'''Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein'''
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===Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15097997 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15097997}}
==About this Structure==
==About this Structure==
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[[Category: Protein design]]
[[Category: Protein design]]
[[Category: Selected binder]]
[[Category: Selected binder]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:12:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:00:11 2008''

Revision as of 06:00, 29 July 2008

Image:1svx.png

Template:STRUCTURE 1svx

Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein

Template:ABSTRACT PUBMED 15097997

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

Page seeded by OCA on Tue Jul 29 09:00:11 2008

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