1zdb: Difference between revisions

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[[Image:1zdb.png|left|200px]]


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==PHAGE-SELECTED MINI PROTEIN A DOMAIN, Z38, NMR, MINIMIZED MEAN STRUCTURE==
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<StructureSection load='1zdb' size='340' side='right'caption='[[1zdb]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1zdb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDB FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdb OCA], [https://pdbe.org/1zdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zdb RCSB], [https://www.ebi.ac.uk/pdbsum/1zdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zdb ProSAT]</span></td></tr>
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== Publication Abstract from PubMed ==
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.


===PHAGE-SELECTED MINI PROTEIN A DOMAIN, Z38, NMR, MINIMIZED MEAN STRUCTURE===
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<ref>PMID:9294166</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 9294166 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_9294166}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDB OCA].
[[Category: Synthetic construct]]
 
[[Category: Starovasnik MA]]
==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:[http://www.ncbi.nlm.nih.gov/pubmed/9294166 9294166]
[[Category: Starovasnik, M A.]]
[[Category: Igg binding domain]]
[[Category: Protein a mimic]]
 
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