1zda
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zdb|1ZDB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zda OCA], [http://www.ebi.ac.uk/pdbsum/1zda PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zda RCSB]</span> | ||
}} | }} | ||
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[[Category: protein a mimic]] | [[Category: protein a mimic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:22 2008'' |
Revision as of 22:34, 30 March 2008
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| Related: | 1ZDB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHAGE-SELECTED MINI PROTEIN A DOMAIN, Z38, NMR, 24 STRUCTURES
Overview
The affinity between molecules depends both on the nature and presentation of the contacts. Here, we observe coupling of functional and structural elements when a protein binding domain is evolved to a smaller functional mimic. Previously, a 38-residue form of the 59-residue B-domain of protein A, termed Z38, was selected by phage display. Z38 contains 13 mutations and binds IgG only 10-fold weaker than the native B-domain. We present the solution structure of Z38 and show that it adopts a tertiary structure remarkably similar to that observed for the first two helices of B-domain in the B-domain/Fc complex [Deisenhofer, J. (1981) Biochemistry 20, 2361-2370], although it is significantly less stable. Based on this structure, we have improved on Z38 by designing a 34-residue disulfide-bonded variant (Z34C) that has dramatically enhanced stability and binds IgG with 9-fold higher affinity. The improved stability of Z34C led to NMR spectra with much greater chemical shift dispersion, resulting in a more precisely determined structure. Z34C, like Z38, has a structure virtually identical to the equivalent region from native protein A domains. The well-defined hydrophobic core of Z34C reveals key structural features that have evolved in this small, functional domain. Thus, the stabilized two-helix peptide, about half the size and having one-third of the remaining residues altered, accurately mimics both the structure and function of the native domain.
About this Structure
1ZDA is a Protein complex structure of sequences from Synthetic construct. Full crystallographic information is available from OCA.
Reference
Structural mimicry of a native protein by a minimized binding domain., Starovasnik MA, Braisted AC, Wells JA, Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10080-5. PMID:9294166
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