6ith
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the transmembrane domain of syndecan 2 in micelles== | |
| + | <StructureSection load='6ith' size='340' side='right' caption='[[6ith]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ith]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ITH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ITH FirstGlance]. <br> | ||
| + | </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=6ith FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ith OCA], [http://pdbe.org/6ith PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ith RCSB], [http://www.ebi.ac.uk/pdbsum/6ith PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ith ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SDC2_HUMAN SDC2_HUMAN]] Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Syndecans are single-span membrane proteins playing important roles in cell-cell and cell-matrix interactions. The transmembrane domain of syndecans is critical for signal transduction across the cell membrane. Here, the structure of the transmembrane domain of syndecan-2 in detergent micelles was investigated using solution NMR spectroscopy. Backbone resonance assignment was obtained, and NMR studies show that the transmembrane domain forms a helix in detergent micelles, which is also supported by the hydrogen and deuterium exchange experiment. A study of the dynamics revealed the rigid structure of the transmembrane domain formed in solution, and paramagnetic relaxation enhancement defined the topology of the transmembrane domain in detergent micelles. This structural analysis may facilitate a better understanding of the role of the syndecan-2 transmembrane domain in signal transduction. | ||
| - | + | Secondary structure and topology of the transmembrane domain of Syndecan-2 in detergent micelles.,Li Q, Ng HQ, Kang C FEBS Lett. 2019 Feb 11. doi: 10.1002/1873-3468.13335. PMID:30742705<ref>PMID:30742705</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ith" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kang, C]] | ||
| + | [[Category: Li, Q]] | ||
| + | [[Category: Ng, H Q]] | ||
| + | [[Category: Dpc]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Micelle]] | ||
Revision as of 15:26, 27 February 2019
Structure of the transmembrane domain of syndecan 2 in micelles
| |||||||||||
Categories: Kang, C | Li, Q | Ng, H Q | Dpc | Membrane protein | Micelle
