1hqj

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[[Image:1hqj.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE==
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The line below this paragraph, containing "STRUCTURE_1hqj", creates the "Structure Box" on the page.
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<StructureSection load='1hqj' size='340' side='right'caption='[[1hqj]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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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'>[[1hqj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1hqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqj OCA], [https://pdbe.org/1hqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqj RCSB], [https://www.ebi.ac.uk/pdbsum/1hqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqj ProSAT]</span></td></tr>
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{{STRUCTURE_1hqj| PDB=1hqj | SCENE= }}
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</table>
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<div style="background-color:#fffaf0;">
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'''CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE'''
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== Publication Abstract from PubMed ==
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==Overview==
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Because of the simplicity and regularity of the alpha-helical coiled coil relative to other structural motifs, it can be conveniently used to clarify the molecular interactions responsible for protein folding and stability. Here we describe the de novo design and characterization of a two heptad-repeat peptide stabilized by a complex network of inter- and intrahelical salt bridges. Circular dichroism spectroscopy and analytical ultracentrifugation show that this peptide is highly alpha-helical and 100% dimeric tinder physiological buffer conditions. Interestingly, the peptide was shown to switch its oligomerization state from a dimer to a trimer upon increasing ionic strength. The correctness of the rational design principles used here is supported by details of the atomic structure of the peptide deduced from X-ray crystallography. The structure of the peptide shows that it is not a molten globule but assumes a unique, native-like conformation. This de novo peptide thus represents an attractive model system for the design of a molecular recognition system.
Because of the simplicity and regularity of the alpha-helical coiled coil relative to other structural motifs, it can be conveniently used to clarify the molecular interactions responsible for protein folding and stability. Here we describe the de novo design and characterization of a two heptad-repeat peptide stabilized by a complex network of inter- and intrahelical salt bridges. Circular dichroism spectroscopy and analytical ultracentrifugation show that this peptide is highly alpha-helical and 100% dimeric tinder physiological buffer conditions. Interestingly, the peptide was shown to switch its oligomerization state from a dimer to a trimer upon increasing ionic strength. The correctness of the rational design principles used here is supported by details of the atomic structure of the peptide deduced from X-ray crystallography. The structure of the peptide shows that it is not a molten globule but assumes a unique, native-like conformation. This de novo peptide thus represents an attractive model system for the design of a molecular recognition system.
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==About this Structure==
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Design of a minimal protein oligomerization domain by a structural approach.,Burkhard P, Meier M, Lustig A Protein Sci. 2000 Dec;9(12):2294-301. PMID:11206050<ref>PMID:11206050</ref>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQJ 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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Design of a minimal protein oligomerization domain by a structural approach., Burkhard P, Meier M, Lustig A, Protein Sci. 2000 Dec;9(12):2294-301. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11206050 11206050]
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</div>
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[[Category: Burkhard, P.]]
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<div class="pdbe-citations 1hqj" style="background-color:#fffaf0;"></div>
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[[Category: Lustig, A.]]
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== References ==
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[[Category: Meier, M.]]
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<references/>
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[[Category: Alpha-helix]]
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__TOC__
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[[Category: Coiled coil]]
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</StructureSection>
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[[Category: De novo design]]
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[[Category: Large Structures]]
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[[Category: Trimer]]
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[[Category: Synthetic construct]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:07:40 2008''
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[[Category: Burkhard P]]
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[[Category: Lustig A]]
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[[Category: Meier M]]

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CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE

PDB ID 1hqj

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