1h0t

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[[Image:1h0t.jpg|left|200px]]
 
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==An affibody in complex with a target protein: structure and coupled folding==
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The line below this paragraph, containing "STRUCTURE_1h0t", creates the "Structure Box" on the page.
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<StructureSection load='1h0t' size='340' side='right'caption='[[1h0t]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h0t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H0T FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1h0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0t OCA], [https://pdbe.org/1h0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h0t RCSB], [https://www.ebi.ac.uk/pdbsum/1h0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0t ProSAT]</span></td></tr>
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{{STRUCTURE_1h0t| PDB=1h0t | SCENE= }}
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</table>
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== Function ==
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'''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''
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[https://www.uniprot.org/uniprot/SPA_STAA8 SPA_STAA8]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/1h0t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h0t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:12594333</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1h0t" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Allard, P.]]
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[[Category: Synthetic construct]]
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[[Category: Berglund, H.]]
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[[Category: Allard P]]
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[[Category: Dincbas-Renqvist, V.]]
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[[Category: Berglund H]]
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[[Category: Hard, T.]]
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[[Category: Dincbas-Renqvist V]]
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[[Category: Hedqvist, A.]]
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[[Category: Hard T]]
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[[Category: Helgstrand, M.]]
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[[Category: Hedqvist A]]
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[[Category: Lendel, C.]]
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[[Category: Helgstrand M]]
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[[Category: Nygren, P A.]]
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[[Category: Lendel C]]
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[[Category: Wahlberg, E.]]
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[[Category: Nygren P-A]]
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[[Category: Affibody]]
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[[Category: Wahlberg E]]
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[[Category: Coupled protein folding]]
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[[Category: Igg binding protein some]]
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[[Category: Induced fit]]
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[[Category: Molecular recognition]]
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[[Category: Molten globule]]
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[[Category: Nmr spectroscopy]]
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[[Category: Protein engineering]]
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[[Category: Protein-protein interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:16:16 2008''
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Current revision

An affibody in complex with a target protein: structure and coupled folding

PDB ID 1h0t

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