1k1f

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[[Image:1k1f.gif|left|200px]]
 
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==Structure of the Bcr-Abl Oncoprotein Oligomerization domain==
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The line below this paragraph, containing "STRUCTURE_1k1f", creates the "Structure Box" on the page.
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<StructureSection load='1k1f' size='340' side='right'caption='[[1k1f]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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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'>[[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>
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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]] 2.2&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1k1f| PDB=1k1f | 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=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>
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</table>
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'''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''
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== Disease ==
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[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).
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== Function ==
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==Overview==
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[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>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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1K1F is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11780146 11780146]
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</div>
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<div class="pdbe-citations 1k1f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ghaffari, S.]]
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[[Category: Ghaffari S]]
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[[Category: Kim, P S.]]
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[[Category: Kim PS]]
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[[Category: Lodish, H.]]
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[[Category: Lodish H]]
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[[Category: Malashkevich, V N.]]
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[[Category: Malashkevich VN]]
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[[Category: Zhao, X.]]
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[[Category: Zhao X]]
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[[Category: Bcr-abl kinase]]
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[[Category: Coiled coil]]
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[[Category: Oligomerization]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:10:52 2008''
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Current revision

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

PDB ID 1k1f

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