1zzp: Difference between revisions

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[[Image:1zzp.gif|left|200px]]
[[Image:1zzp.gif|left|200px]]


{{Structure
<!--
|PDB= 1zzp |SIZE=350|CAPTION= <scene name='initialview01'>1zzp</scene>
The line below this paragraph, containing "STRUCTURE_1zzp", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
or leave the SCENE parameter empty for the default display.
|GENE= ABL1, ABL, JTK7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_1zzp|  PDB=1zzp |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zzp OCA], [http://www.ebi.ac.uk/pdbsum/1zzp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zzp RCSB]</span>
}}


'''Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl'''
'''Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl'''
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[[Category: Superti-Furga, G.]]
[[Category: Superti-Furga, G.]]
[[Category: Wiesner, S.]]
[[Category: Wiesner, S.]]
[[Category: four helix bundle]]
[[Category: Four helix bundle]]
[[Category: nuclear export signal]]
[[Category: Nuclear export signal]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:16:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:48 2008''

Revision as of 18:16, 3 May 2008

File:1zzp.gif

Template:STRUCTURE 1zzp

Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl


OverviewOverview

The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans. Depending on its position within the cell, Bcr-Abl differentially affects cellular growth. However, no structural and molecular details for the anticipated localization determinants are available. We present the NMR structure of the F-actin binding domain (FABD) of Bcr-Abl and its cellular counterpart c-Abl. The FABD forms a compact left-handed four-helix bundle in solution. We show that the nuclear export signal (NES) previously reported in this region is part of the hydrophobic core and nonfunctional in the intact protein. In contrast, we could identify the critical residues of helix alphaIII that are responsible for F-actin binding and cytoskeletal association. We propose that these interactions represent a major determinant for both Bcr-Abl and c-Abl localization.

About this StructureAbout this Structure

1ZZP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl., Hantschel O, Wiesner S, Guttler T, Mackereth CD, Rix LL, Mikes Z, Dehne J, Gorlich D, Sattler M, Superti-Furga G, Mol Cell. 2005 Aug 19;19(4):461-73. PMID:16109371 Page seeded by OCA on Sat May 3 18:16:50 2008

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