2l7h
From Proteopedia
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| - | [[ | + | ==The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503== |
| + | <StructureSection load='2l7h' size='340' side='right' caption='[[2l7h]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2asx 2asx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L7H FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2asw|2asw]], [[2l7i|2l7i]], [[2y0q|2y0q]], [[2y0t|2y0t]], [[2y20|2y20]], [[2y21|2y21]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">af1503, AF_1503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l7h RCSB], [http://www.ebi.ac.uk/pdbsum/2l7h PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | HAMP domains mediate signal transduction in over 7500 enzyme-coupled receptors represented in all kingdoms of life. The HAMP domain of the putative archaeal receptor Af1503 has a parallel, dimeric, four-helical coiled coil structure, but with unusual core packing, related to canonical packing by concerted axial rotation of the helices. This has led to the gearbox model for signal transduction, whereby the alternate packing modes correspond to signaling states. Here we present structures of a series of Af1503 HAMP variants. We show that substitution of a conserved small side chain within the domain core (A291) for larger residues induces a gradual transition in packing mode, involving both changes in helix rotation and bundle shape, which are most prominent at the C-terminal, output end of the domain. These are correlated with activity and ligand response in vitro and in vivo by incorporating Af1503 HAMP into mycobacterial adenylyl cyclase assay systems. | ||
| - | + | The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors.,Ferris HU, Dunin-Horkawicz S, Mondejar LG, Hulko M, Hantke K, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M Structure. 2011 Mar 9;19(3):378-85. PMID:21397188<ref>PMID:21397188</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
| - | [[Category: Coles, M | + | [[Category: Coles, M]] |
| - | [[Category: Hulko, M | + | [[Category: Hulko, M]] |
| - | [[Category: Lupas, A N | + | [[Category: Lupas, A N]] |
| - | [[Category: Martin, J | + | [[Category: Martin, J]] |
[[Category: Complementary x-da]] | [[Category: Complementary x-da]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 13:22, 19 November 2014
The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503
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