View source for 4kfz


==Crystal structure of LMO2 and anti-LMO2 VH complex==
<StructureSection load='4kfz' size='340' side='right'caption='[[4kfz]], [[Resolution|resolution]] 2.80&Aring;' 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]] 2.8&#8491;</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&reg;/PubMed&reg;, 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]]