1cl3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1cl3.gif|left|200px]]
[[Image:1cl3.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1cl3 |SIZE=350|CAPTION= <scene name='initialview01'>1cl3</scene>
+
The line below this paragraph, containing "STRUCTURE_1cl3", 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=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1cl3| PDB=1cl3 | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cl3 OCA], [http://www.ebi.ac.uk/pdbsum/1cl3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cl3 RCSB]</span>
+
-
}}
+
'''MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA'''
'''MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA'''
Line 31: Line 28:
[[Category: Shigesada, K.]]
[[Category: Shigesada, K.]]
[[Category: Werner, M H.]]
[[Category: Werner, M H.]]
-
[[Category: core-binding factor]]
+
[[Category: Core-binding factor]]
-
[[Category: structure from molmol]]
+
[[Category: Structure from molmol]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:51:06 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:44 2008''
+

Revision as of 09:51, 2 May 2008

Template:STRUCTURE 1cl3

MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA


Overview

PEBP2/CBF is a heterodimeric transcription factor essential for genetic regulation of hematopoiesis and osteogenesis. DNA binding by PEBP2/CBF alpha is accomplished by a highly conserved DNA binding domain, the Runt domain (RD), whose structure adopts an S-type immunoglobulin fold when bound to DNA. The supplementary subunit beta enhances DNA binding by the RD in vitro, but its role in the control of gene expression has remained largely unknown in vivo. Chromosome 16 inversion creates a chimeric gene product fusing PEBP2/CBF beta to a portion of the smooth muscle myosin heavy chain (PEBP2/CBF beta-SMMHC) that is causally associated with the onset of acute myeloid leukemia in humans. The three-dimensional structure of PEBP2/CBF beta has been determined in solution and is shown to adopt a fold related to the beta-barrel oligomer binding motif. Direct analysis of a 43.6 kD ternary RD-beta-DNA complex identifies the likely surface of beta in contact with the RD. The structure of PEBP2/CBF beta enables a molecular understanding of the capacity of PEBP2/CBF beta-SMMHC to sequester PEBP2/CBF alpha in the cytoplasm and therefore provides a molecular basis for understanding leukemogenic transformation.

About this Structure

1CL3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular insights into PEBP2/CBF beta-SMMHC associated acute leukemia revealed from the structure of PEBP2/CBF beta., Goger M, Gupta V, Kim WY, Shigesada K, Ito Y, Werner MH, Nat Struct Biol. 1999 Jul;6(7):620-3. PMID:10404215 Page seeded by OCA on Fri May 2 12:51:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools