4ttm

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'''Unreleased structure'''
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==Racemic structure of kalata B1 (kB1)==
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<StructureSection load='4ttm' size='340' side='right' caption='[[4ttm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ttm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TTM FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=DCY:D-CYSTEINE'>DCY</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=DSG:D-ASPARAGINE'>DSG</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>, <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ttm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ttm RCSB], [http://www.ebi.ac.uk/pdbsum/4ttm PDBsum]</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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Cyclic disulfide-rich peptides have exceptional stability and are promising frameworks for drug design. We were interested in obtaining X-ray structures of these peptides to assist in drug design applications, but disulfide-rich peptides can be notoriously difficult to crystallize. To overcome this limitation, we chemically synthesized the L- and D-forms of three prototypic cyclic disulfide-rich peptides: SFTI-1 (14-mer with one disulfide bond), cVc1.1 (22-mer with two disulfide bonds), and kB1 (29-mer with three disulfide bonds) for racemic crystallization studies. Facile crystal formation occurred from a racemic mixture of each peptide, giving structures solved at resolutions from 1.25 A to 1.9 A. Additionally, we obtained the quasi-racemic structures of two mutants of kB1, [G6A]kB1, and [V25A]kB1, which were solved at a resolution of 1.25 A and 2.3 A, respectively. The racemic crystallography approach appears to have broad utility in the structural biology of cyclic peptides.
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The entry 4ttm is ON HOLD until Paper Publication
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Racemic and Quasi-Racemic X-ray Structures of Cyclic Disulfide-Rich Peptide Drug Scaffolds.,Wang CK, King GJ, Northfield SE, Ojeda PG, Craik DJ Angew Chem Int Ed Engl. 2014 Aug 28. doi: 10.1002/anie.201406563. PMID:25168664<ref>PMID:25168664</ref>
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Authors: Wang, C.K., King, G.J., Craik, D.J.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Racemic structure of kalata B1 (kB1)
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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: Craik, D J.]]
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[[Category: King, G J.]]
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[[Category: Wang, C K.]]
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[[Category: Cyclic peptide]]
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[[Category: Disulfide bond]]
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[[Category: Plant protein]]

Revision as of 09:54, 10 September 2014

Racemic structure of kalata B1 (kB1)

4ttm, resolution 1.90Å

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