6cme
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of wild-type ISL2-LID in complex with LHX4-LIM1+2== | |
| + | <StructureSection load='6cme' size='340' side='right'caption='[[6cme]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6cme]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CME FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mmk|3mmk]], [[2rgt|2rgt]], [[2jtn|2jtn]]</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=6cme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cme OCA], [http://pdbe.org/6cme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cme RCSB], [http://www.ebi.ac.uk/pdbsum/6cme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cme ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LHX4_MOUSE LHX4_MOUSE]] May play a critical role in the development of respiratory control mechanisms and in the normal growth and maturation of the lung. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which beta-strands form upon binding. Studies of such complexes, formed by LIM domain proteins and linear motifs in their intrinsically disordered partners, revealed spacer regions between the linear motifs that are relatively flexible but may affect the overall orientation of the binding modules. We demonstrate that mutation of a solvent exposed side chain in the spacer region of an LHX4-ISL2 complex has no significant effect on the structure of the complex, but decreases binding affinity, apparently by increasing flexibility of the linker. | ||
| - | + | Mutation in a flexible linker modulates binding affinity for modular complexes.,Stokes PH, Robertson NO, Silva APG, Estephan T, Trewhella J, Guss JM, Matthews JM Proteins. 2019 May;87(5):425-429. doi: 10.1002/prot.25675. Epub 2019 Mar 9. PMID:30788856<ref>PMID:30788856</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6cme" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Guss, J M]] | ||
| + | [[Category: Matthews, J M]] | ||
| + | [[Category: Silva, A]] | ||
| + | [[Category: Stokes, P H]] | ||
| + | [[Category: Cell-type specification]] | ||
| + | [[Category: Lim-homeodomain]] | ||
| + | [[Category: Neural development]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 07:07, 10 April 2019
Structure of wild-type ISL2-LID in complex with LHX4-LIM1+2
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