4xh3
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4xh3 is ON HOLD Authors: Sun, L.F., Guan, R.F., Chen, Z.C. Description: Mechanistic insights into anchorage of the contractile ring from yeast to h...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Mechanistic insights into anchorage of the contractile ring from yeast to humans== | |
| + | <StructureSection load='4xh3' size='340' side='right'caption='[[4xh3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xh3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XH3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=4xh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh3 OCA], [https://pdbe.org/4xh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4xh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANLN_HUMAN ANLN_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans. | ||
| - | + | Mechanistic insights into the anchorage of the contractile ring by anillin and mid1.,Sun L, Guan R, Lee IJ, Liu Y, Chen M, Wang J, Wu JQ, Chen Z Dev Cell. 2015 May 26;33(4):413-26. doi: 10.1016/j.devcel.2015.03.003. Epub 2015 , May 7. PMID:25959226<ref>PMID:25959226</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4xh3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Guan | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen ZC]] | ||
| + | [[Category: Guan RF]] | ||
| + | [[Category: Sun LF]] | ||
Current revision
Mechanistic insights into anchorage of the contractile ring from yeast to humans
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