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| | ==NMR structure of the human dematin headpiece S74E mutant== | | ==NMR structure of the human dematin headpiece S74E mutant== |
| - | <StructureSection load='1zv6' size='340' side='right' caption='[[1zv6]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='1zv6' size='340' side='right'caption='[[1zv6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zv6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZV6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zv6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZV6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qzp|1qzp]], [[1qqv|1qqv]], [[1vii|1vii]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zv6 OCA], [http://pdbe.org/1zv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zv6 RCSB], [http://www.ebi.ac.uk/pdbsum/1zv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zv6 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zv6 OCA], [https://pdbe.org/1zv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zv6 RCSB], [https://www.ebi.ac.uk/pdbsum/1zv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zv6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DEMA_HUMAN DEMA_HUMAN] Actin-bundling protein. May function in mitogen-activated protein kinase pathway.<ref>PMID:11856323</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Jiang, Z G]] | + | [[Category: Large Structures]] |
| - | [[Category: McKnight, C J]] | + | [[Category: Jiang ZG]] |
| - | [[Category: Actin binding domain]] | + | [[Category: McKnight CJ]] |
| - | [[Category: Dematin headpiece]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
DEMA_HUMAN Actin-bundling protein. May function in mitogen-activated protein kinase pathway.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Dematin is an actin binding protein from the junctional complex of the erythrocyte cytoskeleton. The protein has two actin binding sites and bundles actin filaments in vitro. This actin bundling activity is reversibly regulated by phosphorylation in the carboxyl terminal "headpiece" domain (DHP). DHP is a typical villin-type headpiece actin binding motif and contains a flexible N-terminal loop and an alpha-helical C-terminal subdomain that is phosphorylated at Ser74. The NMR structure of a Ser74-to-Glu mutant (DHPs74e) closely mimics the conformation of phosphorylated DHP. The negative charge at Ser74 does not alter the conformation of the C-terminal subdomain, but attracts the N-terminal loop toward the C terminus, changing the orientation of the N-terminal subdomain. NMR relaxation studies also indicate reduced mobility in the N-terminal loop in DHPs74e. Thus, phosphorylation in DHP serves as a switch controlling the conformational state of DHP and the actin bundling activity of dematin.
A phosphorylation-induced conformation change in dematin headpiece.,Jiang ZG, McKnight CJ Structure. 2006 Feb;14(2):379-87. PMID:16472756[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lutchman M, Kim AC, Cheng L, Whitehead IP, Oh SS, Hanspal M, Boukharov AA, Hanada T, Chishti AH. Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways. Eur J Biochem. 2002 Jan;269(2):638-49. PMID:11856323
- ↑ Jiang ZG, McKnight CJ. A phosphorylation-induced conformation change in dematin headpiece. Structure. 2006 Feb;14(2):379-87. PMID:16472756 doi:10.1016/j.str.2005.11.007
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