2mah: Difference between revisions
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''' | ==Solution structure of Smoothened== | ||
<StructureSection load='2mah' size='340' side='right' caption='[[2mah]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mah]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAH FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">smo, CG11561 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=2mah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mah RCSB], [http://www.ebi.ac.uk/pdbsum/2mah PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Smoothened (Smo) is a member of the Frizzled (FzD) class of G-protein-coupled receptors (GPCRs), and functions as the key transducer in the Hedgehog (Hh) signalling pathway. Smo has an extracellular cysteine-rich domain (CRD), indispensable for its function and downstream Hh signalling. Despite its essential role, the functional contribution of the CRD to Smo signalling has not been clearly elucidated. However, given that the FzD CRD binds to the endogenous Wnt ligand, it has been proposed that the Smo CRD may bind its own endogenous ligand. Here we present the NMR solution structure of the Drosophila Smo CRD, and describe interactions between the glucocorticoid budesonide (Bud) and the Smo CRDs from both Drosophila and human. Our results highlight a function of the Smo CRD, demonstrating its role in binding to small-molecule modulators. | |||
Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling.,Rana R, Carroll CE, Lee HJ, Bao J, Marada S, Grace CR, Guibao CD, Ogden SK, Zheng JJ Nat Commun. 2013;4:2965. doi: 10.1038/ncomms3965. PMID:24351982<ref>PMID:24351982</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drome]] | |||
[[Category: Lee, H.]] | |||
[[Category: Rana, R.]] | |||
[[Category: Zheng, J J.]] | |||
[[Category: Hedgehog]] | |||
[[Category: Oncoprotein]] | |||
[[Category: Smoothened]] | |||
Revision as of 14:42, 18 May 2014
Solution structure of SmoothenedSolution structure of Smoothened
Structural highlights
Publication Abstract from PubMedSmoothened (Smo) is a member of the Frizzled (FzD) class of G-protein-coupled receptors (GPCRs), and functions as the key transducer in the Hedgehog (Hh) signalling pathway. Smo has an extracellular cysteine-rich domain (CRD), indispensable for its function and downstream Hh signalling. Despite its essential role, the functional contribution of the CRD to Smo signalling has not been clearly elucidated. However, given that the FzD CRD binds to the endogenous Wnt ligand, it has been proposed that the Smo CRD may bind its own endogenous ligand. Here we present the NMR solution structure of the Drosophila Smo CRD, and describe interactions between the glucocorticoid budesonide (Bud) and the Smo CRDs from both Drosophila and human. Our results highlight a function of the Smo CRD, demonstrating its role in binding to small-molecule modulators. Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling.,Rana R, Carroll CE, Lee HJ, Bao J, Marada S, Grace CR, Guibao CD, Ogden SK, Zheng JJ Nat Commun. 2013;4:2965. doi: 10.1038/ncomms3965. PMID:24351982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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