4kfz: Difference between revisions
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New page: '''Unreleased structure''' The entry 4kfz is ON HOLD Authors: Sewell, H., Tanaka, T., El Omari, K., Cruz-Migoni, A., Mancini, E.J., Fuentes-Fernandez, N., Chambers, J., Rabbitts, T.H. ... |
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The | ==Crystal structure of LMO2 and anti-LMO2 VH complex== | ||
<StructureSection load='4kfz' size='340' side='right'caption='[[4kfz]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4kfz]] is a 4 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=4KFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KFZ 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4kfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfz OCA], [https://pdbe.org/4kfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kfz RCSB], [https://www.ebi.ac.uk/pdbsum/4kfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kfz ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/RBTN2_HUMAN RBTN2_HUMAN] A chromosomal aberration involving LMO2 may be a cause of a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(11,14)(p13;q11) with TCRD. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RBTN2_HUMAN RBTN2_HUMAN] Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LMO2 was discovered via chromosomal translocations in T-cell leukaemia and shown normally to be essential for haematopoiesis. LMO2 is made up of two LIM only domains (thus it is a LIM-only protein) and forms a bridge in a multi-protein complex. We have studied the mechanism of formation of this complex using a single domain antibody fragment that inhibits LMO2 by sequestering it in a non-functional form. The crystal structure of LMO2 with this antibody fragment has been solved revealing a conformational difference in the positioning and angle between the two LIM domains compared with its normal binding. This contortion occurs by bending at a central helical region of LMO2. This is a unique mechanism for inhibiting an intracellular protein function and the structural contusion implies a model in which newly synthesized, intrinsically disordered LMO2 binds to a partner protein nucleating further interactions and suggests approaches for therapeutic targeting of LMO2. | |||
Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex.,Sewell H, Tanaka T, Omari KE, Mancini EJ, Cruz A, Fernandez-Fuentes N, Chambers J, Rabbitts TH Sci Rep. 2014 Jan 10;4:3643. doi: 10.1038/srep03643. PMID:24407558<ref>PMID:24407558</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4kfz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chambers J]] | |||
[[Category: Cruz-Migoni A]] | |||
[[Category: El Omari K]] | |||
[[Category: Fuentes-Fernandez N]] | |||
[[Category: Mancini EJ]] | |||
[[Category: Rabbitts TH]] | |||
[[Category: Sewell H]] | |||
[[Category: Tanaka T]] | |||
Latest revision as of 15:58, 20 September 2023
Crystal structure of LMO2 and anti-LMO2 VH complex
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