1k1f
From Proteopedia
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| - | + | ==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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K1F FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k1f RCSB], [http://www.ebi.ac.uk/pdbsum/1k1f PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://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). | [[http://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 == | ||
| + | [[http://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> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Ghaffari, S | + | [[Category: Ghaffari, S]] |
| - | [[Category: Kim, P S | + | [[Category: Kim, P S]] |
| - | [[Category: Lodish, H | + | [[Category: Lodish, H]] |
| - | [[Category: Malashkevich, V N | + | [[Category: Malashkevich, V N]] |
| - | [[Category: Zhao, X | + | [[Category: Zhao, X]] |
[[Category: Bcr-abl kinase]] | [[Category: Bcr-abl kinase]] | ||
[[Category: Oligomerization]] | [[Category: Oligomerization]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 12:57, 18 December 2014
Structure of the Bcr-Abl Oncoprotein Oligomerization domain
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