1h0t: Difference between revisions

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'''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''<br />
{{Structure
|PDB= 1h0t |SIZE=350|CAPTION= <scene name='initialview01'>1h0t</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''
 


==Overview==
==Overview==
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==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0T OCA].  
1H0T is a [[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].  


==Reference==
==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]
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://www.ncbi.nlm.nih.gov/pubmed/12594333 12594333]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: affibody]]
[[Category: affibody]]
[[Category: coupled protein folding]]
[[Category: coupled protein folding]]
[[Category: igg binding protein a]]
[[Category: igg binding protein some]]
[[Category: induced fit]]
[[Category: induced fit]]
[[Category: molecular recognition]]
[[Category: molecular recognition]]
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[[Category: nmr spectroscopy]]
[[Category: nmr spectroscopy]]
[[Category: protein engineering]]
[[Category: protein engineering]]
[[Category: protein-protein interactions]]
[[Category: protein-protein interaction]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:39 2008''

Revision as of 12:30, 20 March 2008

File:1h0t.jpg


PDB ID 1h0t

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AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING


OverviewOverview

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 StructureAbout this Structure

1H0T is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

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

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