1h0t
From Proteopedia
(New page: 200px<br /><applet load="1h0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h0t" /> '''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN...) |
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| - | [[Image:1h0t.jpg|left|200px]]<br /><applet load="1h0t" size=" | + | [[Image:1h0t.jpg|left|200px]]<br /><applet load="1h0t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h0t" /> | caption="1h0t" /> | ||
'''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''<br /> | '''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''<br /> | ||
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| + | ==Overview== | ||
| + | Combinatorial protein engineering provides powerful means for functional selection of novel binding proteins. One class of engineered binding proteins, denoted affibodies, is based on the three-helix scaffold of the Z domain derived from staphylococcal protein A. The Z(SPA-1) affibody has been selected from a phage-displayed library as a binder to protein A. Z(SPA-1) also binds with micromolar affinity to its own ancestor, the Z domain. We have characterized the Z(SPA-1) affibody in its uncomplexed state and determined the solution structure of a Z:Z(SPA-1) protein-protein complex. Uncomplexed Z(SPA-1) behaves as an aggregation-prone molten globule, but folding occurs on binding, and the original (Z) three-helix bundle scaffold is fully formed in the complex. The structural basis for selection and strong binding is a large interaction interface with tight steric and polar/nonpolar complementarity that directly involves 10 of 13 mutated amino acid residues on Z(SPA-1). We also note similarities in how the surface of the Z domain responds by induced fit to binding of Z(SPA-1) and Ig Fc, respectively, suggesting that the Z(SPA-1) affibody is capable of mimicking the morphology of the natural binding partner for the Z domain. | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http:// | + | 1H0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0T OCA]. |
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| + | ==Reference== | ||
| + | An affibody in complex with a target protein: structure and coupled folding., Wahlberg E, Lendel C, Helgstrand M, Allard P, Dincbas-Renqvist V, Hedqvist A, Berglund H, Nygren PA, Hard T, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3185-90. Epub 2003 Feb 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12594333 12594333] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: Helgstrand, M.]] | [[Category: Helgstrand, M.]] | ||
[[Category: Lendel, C.]] | [[Category: Lendel, C.]] | ||
| - | [[Category: Nygren, P | + | [[Category: Nygren, P A.]] |
[[Category: Wahlberg, E.]] | [[Category: Wahlberg, E.]] | ||
[[Category: affibody]] | [[Category: affibody]] | ||
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[[Category: protein-protein interactions]] | [[Category: protein-protein interactions]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:15 2008'' |
Revision as of 10:56, 21 February 2008
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AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING
Overview
Combinatorial protein engineering provides powerful means for functional selection of novel binding proteins. One class of engineered binding proteins, denoted affibodies, is based on the three-helix scaffold of the Z domain derived from staphylococcal protein A. The Z(SPA-1) affibody has been selected from a phage-displayed library as a binder to protein A. Z(SPA-1) also binds with micromolar affinity to its own ancestor, the Z domain. We have characterized the Z(SPA-1) affibody in its uncomplexed state and determined the solution structure of a Z:Z(SPA-1) protein-protein complex. Uncomplexed Z(SPA-1) behaves as an aggregation-prone molten globule, but folding occurs on binding, and the original (Z) three-helix bundle scaffold is fully formed in the complex. The structural basis for selection and strong binding is a large interaction interface with tight steric and polar/nonpolar complementarity that directly involves 10 of 13 mutated amino acid residues on Z(SPA-1). We also note similarities in how the surface of the Z domain responds by induced fit to binding of Z(SPA-1) and Ig Fc, respectively, suggesting that the Z(SPA-1) affibody is capable of mimicking the morphology of the natural binding partner for the Z domain.
About this Structure
1H0T is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
An affibody in complex with a target protein: structure and coupled folding., Wahlberg E, Lendel C, Helgstrand M, Allard P, Dincbas-Renqvist V, Hedqvist A, Berglund H, Nygren PA, Hard T, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3185-90. Epub 2003 Feb 19. PMID:12594333
Page seeded by OCA on Thu Feb 21 12:56:15 2008
Categories: Single protein | Staphylococcus aureus | Allard, P. | Berglund, H. | Dincbas-Renqvist, V. | Hard, T. | Hedqvist, A. | Helgstrand, M. | Lendel, C. | Nygren, P A. | Wahlberg, E. | Affibody | Coupled protein folding | Igg binding protein a | Induced fit | Molecular recognition | Molten globule | Nmr spectroscopy | Protein engineering | Protein-protein interactions
