2kya

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[[Image:2kya.png|left|200px]]
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==Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34==
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<StructureSection load='2kya' size='340' side='right' caption='[[2kya]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2kya]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KYA FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kya OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kya RCSB], [http://www.ebi.ac.uk/pdbsum/2kya PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/ky/2kya_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/chain_selection.php?pdb_ID=2ata 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 ==
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The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an alpha-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.
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{{STRUCTURE_2kya| PDB=2kya | SCENE= }}
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Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE(1-34).,Houssen WE, Wright SH, Kalverda AP, Thompson GS, Kelly SM, Jaspars M Chembiochem. 2010 Aug 16. PMID:20715266<ref>PMID:20715266</ref>
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===Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34===
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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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{{ABSTRACT_PUBMED_20715266}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2kya]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYA OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020715266</ref><references group="xtra"/>
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[[Category: Houssen, W E.]]
[[Category: Houssen, W E.]]
[[Category: Jaspars, M.]]
[[Category: Jaspars, M.]]

Revision as of 11:24, 20 October 2014

Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34

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