1y47

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(New page: 200px<br /><applet load="1y47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y47, resolution 2.70&Aring;" /> '''Structural studies o...)
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[[Image:1y47.gif|left|200px]]<br /><applet load="1y47" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y47, resolution 2.70&Aring;" />
 
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'''Structural studies of designed alpha-helical hairpins'''<br />
 
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==Overview==
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==Structural studies of designed alpha-helical hairpins==
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Although the analysis and design of turns that connect the strands in, antiparallel beta-hairpins has reached an advanced state, much less is, known concerning turns between antiparallel helices in helical hairpins., We have conducted an analysis of the structures and sequence preferences, of two types of interhelical turns, each of which connects the two helices, by a two-residue linker in an alphaL-beta conformation. Based on this, analysis, it became apparent that the turn introduced into a designed, four-helix bundle protein, DF1, did not occur within an optimal structural, context. DF1 is a dimeric model for the diiron class of proteins. A longer, loop with a beta-alphaR-beta conformation was inserted between two helices, in the protein, and a sequence was chosen to stabilize its conformation., X-ray crystallography and NMR analysis of the protein showed the structure, to be in excellent agreement with design.
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<StructureSection load='1y47' size='340' side='right'caption='[[1y47]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y47]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y47 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=1y47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y47 OCA], [https://pdbe.org/1y47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y47 RCSB], [https://www.ebi.ac.uk/pdbsum/1y47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y47 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.
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==About this Structure==
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Analysis and design of turns in alpha-helical hairpins.,Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF J Mol Biol. 2005 Mar 11;346(5):1441-54. Epub 2005 Jan 13. PMID:15713492<ref>PMID:15713492</ref>
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1Y47 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y47 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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Analysis and design of turns in alpha-helical hairpins., Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF, J Mol Biol. 2005 Mar 11;346(5):1441-54. Epub 2005 Jan 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15713492 15713492]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1y47" style="background-color:#fffaf0;"></div>
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[[Category: DeGrado, W.F.]]
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== References ==
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[[Category: Engel, D.E.]]
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<references/>
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[[Category: Geremia, S.]]
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__TOC__
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[[Category: Lahr, S.J.]]
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</StructureSection>
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[[Category: Lombardi, A.]]
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[[Category: Large Structures]]
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[[Category: Maglio, O.]]
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[[Category: DeGrado WF]]
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[[Category: North, B.]]
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[[Category: Engel DE]]
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[[Category: Stayrook, S.E.]]
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[[Category: Geremia S]]
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[[Category: CD]]
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[[Category: Lahr SJ]]
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[[Category: diiron proteins]]
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[[Category: Lombardi A]]
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[[Category: helical hairpin]]
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[[Category: Maglio O]]
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[[Category: protein design]]
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[[Category: North B]]
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[[Category: turns]]
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[[Category: Stayrook SE]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:27:41 2007''
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Current revision

Structural studies of designed alpha-helical hairpins

PDB ID 1y47

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