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5oc7

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Revision as of 12:21, 26 August 2020

Crystal structure of the pleckstrin-homology domain of Bcr-Abl in complex with monobody Mb(Bcr-PH_4).

Structural highlights

5oc7 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
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 two isoforms of the Bcr-Abl tyrosine kinase, p210 and p190, are associated with different leukemias and have a dramatically different signaling network, despite similar kinase activity. To provide a molecular rationale for these observations, we study the Dbl-homology (DH) and Pleckstrin-homology (PH) domains of Bcr-Abl p210, which constitute the only structural differences to p190. Here we report high-resolution structures of the DH and PH domains and characterize conformations of the DH-PH unit in solution. Our structural and functional analyses show no evidence that the DH domain acts as a guanine nucleotide exchange factor, whereas the PH domain binds to various phosphatidylinositol-phosphates. PH-domain mutants alter subcellular localization and result in decreased interactions with p210-selective interaction partners. Hence, the PH domain, but not the DH domain, plays an important role in the formation of the differential p210 and p190 Bcr-Abl signaling networks.

Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase.,Reckel S, Gehin C, Tardivon D, Georgeon S, Kukenshoner T, Lohr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Guntert P, Dotsch V, Koide S, Gavin AC, Hantschel O Nat Commun. 2017 Dec 13;8(1):2101. doi: 10.1038/s41467-017-02313-6. PMID:29235475^[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
↑ Reckel S, Gehin C, Tardivon D, Georgeon S, Kukenshoner T, Lohr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Guntert P, Dotsch V, Koide S, Gavin AC, Hantschel O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun. 2017 Dec 13;8(1):2101. doi: 10.1038/s41467-017-02313-6. PMID:29235475 doi:http://dx.doi.org/10.1038/s41467-017-02313-6

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/5oc7"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the pleckstrin-homology domain of Bcr-Abl in complex with monobody Mb(Bcr-PH_4).==
-<StructureSection load='5oc7' size='340' side='right' caption='[[5oc7]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+<StructureSection load='5oc7' size='340' side='right'caption='[[5oc7]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5oc7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OC7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5oc7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OC7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IP2:D-MYO-INOSITOL-4,5-BISPHOSPHATE'>IP2</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IP2:D-MYO-INOSITOL-4,5-BISPHOSPHATE'>IP2</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=5oc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc7 OCA], [http://pdbe.org/5oc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oc7 RCSB], [http://www.ebi.ac.uk/pdbsum/5oc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc7 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5oc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc7 OCA], [http://pdbe.org/5oc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oc7 RCSB], [http://www.ebi.ac.uk/pdbsum/5oc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc7 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 24: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Hantschel, O]]
 [[Category: Pojer, F]]

5oc7

From Proteopedia

Revision as of 12:21, 26 August 2020

Crystal structure of the pleckstrin-homology domain of Bcr-Abl in complex with monobody Mb(Bcr-PH_4).

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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