2mbb: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Solution Structure of the human Polymerase iota UBM1-Ubiquitin Complex==

== Structural highlights ==

<table><tr><td colspan='2'>[[2mbb]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MBB FirstGlance]. <br>

</td></tr><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=2mbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mbb RCSB], [http://www.ebi.ac.uk/pdbsum/2mbb PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of (1)JHC scalar couplings and limited chemical shift dispersion in the indirect proton dimension, it is difficult to obtain reliable and complete assignments of interfacial NOEs. Here, we demonstrate a strategy that combines selective labeling and high-resolution 4-D NOE spectroscopy with sparse sampling for reliable identification and assignment of intermolecular NOEs. Spectral subtraction of component-labeled complexes from a uniformly-labeled protein complex yields an "omit" spectrum containing positive intermolecular NOEs with little signal degeneracy. Such a strategy can be broadly applied to unbiased detection, assignment and presentation of intermolecular NOEs of protein complexes.

~~The entry 2mbb is ON HOLD until Paper Publication~~

Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes.,Wang S, Zhou P J Biomol NMR. 2014 Jun;59(2):51-6. doi: 10.1007/s10858-014-9834-2. Epub 2014 May , 1. PMID:24789524<ref>PMID:24789524</ref>

~~Authors~~: Wang, S., Zhou, P.

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: ~~Solution Structure of the human~~ Polymerase iota ~~UBM1-~~Ubiquitin ~~Complex~~

== References ==

__TOC__

</StructureSection>

[[Category: Wang, S.]]

[[Category: Zhou, P.]]

[[Category: Polymerase iota]]

[[Category: Signaling protein]]

[[Category: Transferase]]

[[Category: Ubiquitin]]

[[Category: Ubm]]

[[Category: Ubm1]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Solution Structure of the human Polymerase iota UBM1-Ubiquitin Complex==
+<StructureSection load='2mbb' size='340' side='right' caption='[[2mbb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mbb]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MBB FirstGlance]. <br>
+</td></tr><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=2mbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mbb RCSB], [http://www.ebi.ac.uk/pdbsum/2mbb PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of (1)JHC scalar couplings and limited chemical shift dispersion in the indirect proton dimension, it is difficult to obtain reliable and complete assignments of interfacial NOEs. Here, we demonstrate a strategy that combines selective labeling and high-resolution 4-D NOE spectroscopy with sparse sampling for reliable identification and assignment of intermolecular NOEs. Spectral subtraction of component-labeled complexes from a uniformly-labeled protein complex yields an "omit" spectrum containing positive intermolecular NOEs with little signal degeneracy. Such a strategy can be broadly applied to unbiased detection, assignment and presentation of intermolecular NOEs of protein complexes.
-The entry 2mbb is ON HOLD  until Paper Publication
+Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes.,Wang S, Zhou P J Biomol NMR. 2014 Jun;59(2):51-6. doi: 10.1007/s10858-014-9834-2. Epub 2014 May , 1. PMID:24789524<ref>PMID:24789524</ref>
-Authors: Wang, S., Zhou, P.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Solution Structure of the human Polymerase iota UBM1-Ubiquitin Complex
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Wang, S.]]
+[[Category: Zhou, P.]]
+[[Category: Polymerase iota]]
+[[Category: Signaling protein]]
+[[Category: Transferase]]
+[[Category: Ubiquitin]]
+[[Category: Ubm]]
+[[Category: Ubm1]]