1k1f
From Proteopedia
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- | [[Image:1k1f.png|left|200px]] | ||
- | + | ==Structure of the Bcr-Abl Oncoprotein Oligomerization domain== | |
+ | <StructureSection load='1k1f' size='340' side='right'caption='[[1k1f]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1k1f]] is a 8 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=1K1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1F 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]] 2.2Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1k1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1f OCA], [https://pdbe.org/1k1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1f RCSB], [https://www.ebi.ac.uk/pdbsum/1k1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1f ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/BCR_HUMAN BCR_HUMAN] Note=A chromosomal aberration involving BCR is a cause of chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/BCR_HUMAN BCR_HUMAN] GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity.<ref>PMID:1903516</ref> <ref>PMID:1657398</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Bcr-Abl oncoprotein is responsible for a wide range of human leukemias, including most cases of Philadelphia chromosome-positive chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for oncogenicity. We determined the crystal structure of the N-terminal oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a novel mode of oligomer formation. Two N-shaped monomers dimerize by swapping N-terminal helices and by forming an antiparallel coiled coil between C-terminal helices. Two dimers then stack onto each other to form a tetramer. The Bcr1-72 structure provides a basis for the design of inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl oligomerization. | ||
- | + | Structure of the Bcr-Abl oncoprotein oligomerization domain.,Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS Nat Struct Biol. 2002 Feb;9(2):117-20. PMID:11780146<ref>PMID:11780146</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1k1f" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Ghaffari | + | [[Category: Large Structures]] |
- | [[Category: Kim | + | [[Category: Ghaffari S]] |
- | [[Category: Lodish | + | [[Category: Kim PS]] |
- | [[Category: Malashkevich | + | [[Category: Lodish H]] |
- | [[Category: Zhao | + | [[Category: Malashkevich VN]] |
- | + | [[Category: Zhao X]] | |
- | + | ||
- | + |
Current revision
Structure of the Bcr-Abl Oncoprotein Oligomerization domain
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