2rpv: Difference between revisions
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[[Image: | ==Solution Structure of GB1 with LBT probe== | ||
<StructureSection load='2rpv' size='340' side='right' caption='[[2rpv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._'group_g' Streptococcus sp. 'group g']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RPV FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LA:LANTHANUM+(III)+ION'>LA</scene><br> | |||
<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=2rpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rpv RCSB], [http://www.ebi.ac.uk/pdbsum/2rpv PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rp/2rpv_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Paramagnetic lanthanide ions fixed in a protein frame induce several paramagnetic effects such as pseudo-contact shifts and residual dipolar couplings. These effects provide long-range distance and angular information for proteins and, therefore, are valuable in protein structural analysis. However, until recently this approach had been restricted to metal-binding proteins, but now it has become applicable to non-metalloproteins through the use of a lanthanide-binding tag. Here we report a lanthanide-binding peptide tag anchored via two points to the target proteins. Compared to conventional single-point attached tags, the two-point linked tag provides two to threefold stronger anisotropic effects. Though there is slight residual mobility of the lanthanide-binding tag, the present tag provides a higher anisotropic paramagnetic effect. | |||
Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect.,Saio T, Ogura K, Yokochi M, Kobashigawa Y, Inagaki F J Biomol NMR. 2009 Jul;44(3):157-66. Epub 2009 May 26. PMID:19468839<ref>PMID:19468839</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Streptococcus sp. 'group g']] | [[Category: Streptococcus sp. 'group g']] | ||
[[Category: Inagaki, F.]] | [[Category: Inagaki, F.]] | ||
Revision as of 02:18, 1 October 2014
Solution Structure of GB1 with LBT probe
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