1k1f

From Proteopedia

(Difference between revisions)

Revision as of 08:44, 21 April 2021

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Structural highlights

1k1f is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Diekmann D, Brill S, Garrett MD, Totty N, Hsuan J, Monfries C, Hall C, Lim L, Hall A. Bcr encodes a GTPase-activating protein for p21rac. Nature. 1991 May 30;351(6325):400-2. PMID:1903516 doi:http://dx.doi.org/10.1038/351400a0
↑ Maru Y, Witte ON. The BCR gene encodes a novel serine/threonine kinase activity within a single exon. Cell. 1991 Nov 1;67(3):459-68. PMID:1657398
↑ Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS. Structure of the Bcr-Abl oncoprotein oligomerization domain. Nat Struct Biol. 2002 Feb;9(2):117-20. PMID:11780146 doi:10.1038/nsb747

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k1f"

@@ Line 3: / Line 3: @@
 <StructureSection load='1k1f' size='340' side='right'caption='[[1k1f]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k1f]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<table><tr><td colspan='2'>[[1k1f]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='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://pdbe.org/1k1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k1f RCSB], [http://www.ebi.ac.uk/pdbsum/1k1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1f ProSAT]</span></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 ==
-[[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).
+[[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 ==
-[[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>
+[[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 ==

1k1f

From Proteopedia

Revision as of 08:44, 21 April 2021

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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