2obg
From Proteopedia
(New page: 200px<br /> <applet load="2obg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2obg, resolution 2.35Å" /> '''Crystal Structure o...) |
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caption="2obg, resolution 2.35Å" /> | caption="2obg, resolution 2.35Å" /> | ||
'''Crystal Structure of Monobody MBP-74/Maltose Binding Protein Fusion Complex'''<br /> | '''Crystal Structure of Monobody MBP-74/Maltose Binding Protein Fusion Complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_synthetic Escherichia coli, synthetic]. Full crystallographic information is available from [http:// | + | 2OBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_synthetic Escherichia coli, synthetic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: domain swapping]] | [[Category: domain swapping]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:34 2008'' |
Revision as of 13:19, 23 January 2008
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Crystal Structure of Monobody MBP-74/Maltose Binding Protein Fusion Complex
Overview
High degrees of sequence and conformation complexity found in natural, protein interaction interfaces are generally considered essential for, achieving tight and specific interactions. However, it has been, demonstrated that specific antibodies can be built by using an interface, with a binary code consisting of only Tyr and Ser. This surprising result, might be attributed to yet undefined properties of the antibody scaffold, that uniquely enhance its capacity for target binding. In this work we, tested the generality of the binary-code interface by engineering binding, proteins based on a single-domain scaffold. We show that Tyr/Ser, binary-code interfaces consisting of only 15-20 positions within a, fibronectin type III domain (FN3; 95 residues) are capable of producing, specific binding proteins (termed "monobodies") with a low-nanomolar K(d)., A 2.35-A x-ray crystal structure of a monobody in complex with its target, maltose-binding protein, and mutation analysis revealed dominant, contributions of Tyr residues to binding as well as striking molecular, mimicry of a maltose-binding protein substrate, beta-cyclodextrin, by the, Tyr/Ser binary interface. This work suggests that an interaction interface, with low chemical diversity but with significant conformational diversity, is generally sufficient for tight and specific molecular recognition, providing fundamental insights into factors governing protein-protein, interactions.
About this Structure
2OBG is a Single protein structure of sequence from Escherichia coli, synthetic. Full crystallographic information is available from OCA.
Reference
High-affinity single-domain binding proteins with a binary-code interface., Koide A, Gilbreth RN, Esaki K, Tereshko V, Koide S, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6632-7. Epub 2007 Apr 9. PMID:17420456
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