4wms: Difference between revisions

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-'''Unreleased structure'''
+==STRUCTURE OF APO MBP-MCL1 AT 1.9A==
+<StructureSection load='4wms' size='340' side='right' caption='[[4wms]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WMS FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wmt|4wmt]], [[4wmu|4wmu]], [[4wmv|4wmv]], [[4wmw|4wmw]], [[4wmx|4wmx]], [[4wmr|4wmr]]</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=4wms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wms OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wms RCSB], [http://www.ebi.ac.uk/pdbsum/4wms PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.
-The entry 4wms is ON HOLD  until Paper Publication
+A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.,Clifton MC, Dranow DM, Leed A, Fulroth B, Fairman JW, Abendroth J, Atkins KA, Wallace E, Fan D, Xu G, Ni ZJ, Daniels D, Van Drie J, Wei G, Burgin AB, Golub TR, Hubbard BK, Serrano-Wu MH PLoS One. 2015 Apr 24;10(4):e0125010. doi: 10.1371/journal.pone.0125010., eCollection 2015. PMID:25909780<ref>PMID:25909780</ref>
-Authors: Clifton, M.C., Dranow, D.M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Dranow, D.M]]
+__TOC__
-[[Category: Clifton, M.C]]
+</StructureSection>
+[[Category: Clifton, M C]]
+[[Category: Dranow, D M]]
+[[Category: Apoptosis]]
+[[Category: Chimera protein]]
+[[Category: Protein-protein interaction]]