1na0: Difference between revisions

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<StructureSection load='1na0' size='340' side='right'caption='[[1na0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1na0' size='340' side='right'caption='[[1na0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1na0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NA0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1na0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NA0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPT:ISOPROPYL-1-BETA-D-THIOGALACTOSIDE'>IPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1na3|1na3]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPT:ISOPROPYL-1-BETA-D-THIOGALACTOSIDE'>IPT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1na0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1na0 OCA], [https://pdbe.org/1na0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1na0 RCSB], [https://www.ebi.ac.uk/pdbsum/1na0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1na0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1na0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1na0 OCA], [https://pdbe.org/1na0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1na0 RCSB], [https://www.ebi.ac.uk/pdbsum/1na0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1na0 ProSAT]</span></td></tr>
</table>
</table>
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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/main_output.php?pdb_ID=1na0 ConSurf].
</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/main_output.php?pdb_ID=1na0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that occurs in over 300 different proteins. In the different proteins, three to sixteen or more TPR motifs occur in tandem arrays and function to mediate protein-protein interactions. The binding specificity of each TPR protein is different, although the underlying structural motif is the same. Here we describe a statistical approach to the design of an idealized TPR motif. We present the high-resolution X-ray crystal structures (to 1.55 and 1.6 A) of designed TPR proteins and describe their solution properties and stability. A detailed analysis of these structures provides an understanding of the TPR motif, how it is repeated to give helical arrays with different superhelical twists, and how a very stable framework may be constructed for future functional designs.
Design of stable alpha-helical arrays from an idealized TPR motif.,Main ER, Xiong Y, Cocco MJ, D'Andrea L, Regan L Structure. 2003 May;11(5):497-508. PMID:12737816<ref>PMID:12737816</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1na0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Miscellaneous nucleic acid]]
[[Category: Unidentified]]
[[Category: Andrea, L D]]
[[Category: Cocco M]]
[[Category: Cocco, M]]
[[Category: D'Andrea L]]
[[Category: Main, E]]
[[Category: Main E]]
[[Category: Regan, L]]
[[Category: Regan L]]
[[Category: Xiong, Y]]
[[Category: Xiong Y]]
[[Category: De novo protein]]
[[Category: Design]]
[[Category: Tpr]]
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