1h0t: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0t OCA], [http://www.ebi.ac.uk/pdbsum/1h0t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h0t RCSB]</span> | |||
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[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
''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 20:55:20 2008'' | ||
Revision as of 20:55, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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 some
- Induced fit
- Molecular recognition
- Molten globule
- Nmr spectroscopy
- Protein engineering
- Protein-protein interaction