2dfy

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{{Seed}}
 
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[[Image:2dfy.png|left|200px]]
 
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==Crystal structure of a cyclized protein fusion of LMO4 LIM domains 1 and 2 with the LIM interacting domain of LDB1==
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The line below this paragraph, containing "STRUCTURE_2dfy", creates the "Structure Box" on the page.
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<StructureSection load='2dfy' size='340' side='right'caption='[[2dfy]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2dfy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DFY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2dfy| PDB=2dfy | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfy OCA], [https://pdbe.org/2dfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dfy RCSB], [https://www.ebi.ac.uk/pdbsum/2dfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dfy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LMO4_MOUSE LMO4_MOUSE] Probable transcriptional factor.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/2dfy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dfy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The study of protein-protein interactions can be hampered by the instability of one or more of the protein complex components. In this study, we showed that intein-mediated cyclization can be used to engineer an artificial intramolecular cyclic protein complex between two interacting proteins: the largely unstable LIM-only protein 4 (LMO4) and an unstructured domain of LIM domain binding protein 1 (ldb1). The X-ray structure of the cyclic complex is identical to noncyclized versions of the complex. Chemical and thermal denaturation assays using intrinsic tryptophan fluorescence and dynamic light scattering were used to compare the relative stabilities of the cyclized complex, the intermolecular (or free) complex, and two linear versions of the intramolecular complex (in which the interacting domains of LMO4 and ldb1 were fused, via a flexible linker, in either orientation). In terms of resistance to denaturation, the cyclic complex is the most stable variant and the intermolecular complex is the least stable; however, the two linear intramolecular variants show significant differences in stability. These differences appear to be related to the relative contact order (the average distance in sequence between residues that make contacts within a structure) of key binding residues at the interface of the two proteins. Thus, the restriction of the more stable component of a complex may enhance stability to a greater extent than restraining less stable components.
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===Crystal structure of a cyclized protein fusion of LMO4 LIM domains 1 and 2 with the LIM interacting domain of LDB1===
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Stabilization of a binary protein complex by intein-mediated cyclization.,Jeffries CM, Graham SC, Stokes PH, Collyer CA, Guss JM, Matthews JM Protein Sci. 2006 Nov;15(11):2612-8. Epub 2006 Sep 25. PMID:17001033<ref>PMID:17001033</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17001033}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2dfy" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17001033 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17001033}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2DFY is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFY OCA].
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==Reference==
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<ref group="xtra">PMID:17001033</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Collyer, C A.]]
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[[Category: Collyer CA]]
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[[Category: Graham, S C.]]
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[[Category: Graham SC]]
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[[Category: Guss, J M.]]
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[[Category: Guss JM]]
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[[Category: Jeffries, C M.J.]]
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[[Category: Jeffries CMJ]]
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[[Category: Matthews, J M.]]
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[[Category: Matthews JM]]
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[[Category: Circular protein]]
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[[Category: Lim domain]]
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[[Category: Lim only protein]]
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[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:43:57 2009''
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Current revision

Crystal structure of a cyclized protein fusion of LMO4 LIM domains 1 and 2 with the LIM interacting domain of LDB1

PDB ID 2dfy

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