2bkg

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[[Image:2bkg.png|left|200px]]
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==CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN==
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<StructureSection load='2bkg' size='340' side='right' caption='[[2bkg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bkg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BKG FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k1a|1k1a]], [[1k1b|1k1b]], [[1mj0|1mj0]], [[1n0q|1n0q]], [[1n0r|1n0r]]</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=2bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bkg RCSB], [http://www.ebi.ac.uk/pdbsum/2bkg 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/bk/2bkg_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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Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.
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{{STRUCTURE_2bkg| PDB=2bkg | SCENE= }}
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Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability.,Binz HK, Kohl A, Pluckthun A, Grutter MG Proteins. 2006 Nov 1;65(2):280-4. PMID:16493627<ref>PMID:16493627</ref>
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===CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN===
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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_16493627}}
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==About this Structure==
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[[2bkg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA].
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==See Also==
==See Also==
*[[Ankyrin|Ankyrin]]
*[[Ankyrin|Ankyrin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016493627</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Binz, H K.]]
[[Category: Binz, H K.]]
[[Category: Grutter, M G.]]
[[Category: Grutter, M G.]]

Revision as of 03:11, 29 September 2014

CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN

2bkg, resolution 1.90Å

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