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[[ | ==Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY== | ||
<StructureSection load='2lag' size='340' side='right' caption='[[2lag]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lag]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LAG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kz1|1kz1]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNAR2, IFNABR, IFNARB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), IFNA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2lag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lag RCSB], [http://www.ebi.ac.uk/pdbsum/2lag PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NMR detection of intermolecular interactions between protons in large protein complexes is very challenging since it is difficult to distinguish between weak NOEs from intermolecular interactions and the much larger number of strong intramolecular NOEs. This challenging task is exacerbated by the decrease in signal-to-noise ratio in the often used isotope-edited and isotope-filtered experiments as a result of enhanced T2 relaxation. Here we calculate a double difference spectrum that shows exclusively intermolecular NOEs and manifests the good signal-to-noise ratio in 2D homonuclear NOESY spectra even for large proteins. The method is straightforward and results in a complete picture of all intermolecular interactions involving non exchangeable protons. Ninety seven such 1H-1H NOEs were assigned for the 44 KDa interferon-alpha2/IFNAR2 complex and used for docking these two proteins. The symmetry of the difference spectrum, its superb resolution and unprecedented signal-to-noise ratio in this large protein/receptor complex suggest that this method is generally applicable to study large biopolymeric complexes. | |||
Observation of intermolecular interactions in large protein complexes by 2D-double difference NOESY: application to the 44 kDa interferon-receptor complex.,Nudelman I, Akabayov SR, Scherf T, Anglister J J Am Chem Soc. 2011 Aug 8. PMID:21819146<ref>PMID:21819146</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Interferon|Interferon]] | *[[Interferon|Interferon]] | ||
*[[Interferon receptor|Interferon receptor]] | |||
*[[Multiple sclerosis|Multiple sclerosis]] | *[[Multiple sclerosis|Multiple sclerosis]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Akabayov, S R.]] | [[Category: Akabayov, S R.]] | ||
Revision as of 08:44, 29 September 2014
Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESYStructure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY
Structural highlights
Publication Abstract from PubMedNMR detection of intermolecular interactions between protons in large protein complexes is very challenging since it is difficult to distinguish between weak NOEs from intermolecular interactions and the much larger number of strong intramolecular NOEs. This challenging task is exacerbated by the decrease in signal-to-noise ratio in the often used isotope-edited and isotope-filtered experiments as a result of enhanced T2 relaxation. Here we calculate a double difference spectrum that shows exclusively intermolecular NOEs and manifests the good signal-to-noise ratio in 2D homonuclear NOESY spectra even for large proteins. The method is straightforward and results in a complete picture of all intermolecular interactions involving non exchangeable protons. Ninety seven such 1H-1H NOEs were assigned for the 44 KDa interferon-alpha2/IFNAR2 complex and used for docking these two proteins. The symmetry of the difference spectrum, its superb resolution and unprecedented signal-to-noise ratio in this large protein/receptor complex suggest that this method is generally applicable to study large biopolymeric complexes. Observation of intermolecular interactions in large protein complexes by 2D-double difference NOESY: application to the 44 kDa interferon-receptor complex.,Nudelman I, Akabayov SR, Scherf T, Anglister J J Am Chem Soc. 2011 Aug 8. PMID:21819146[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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