1cl3: Difference between revisions
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'''MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA''' | {{Structure | ||
|PDB= 1cl3 |SIZE=350|CAPTION= <scene name='initialview01'>1cl3</scene> | |||
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'''MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CL3 is a [ | 1CL3 is a [[Single protein]] structure of 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=1CL3 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10404215 10404215] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: structure from molmol]] | [[Category: structure from molmol]] | ||
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Revision as of 11:25, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Myeloid leukemia, acute, M4Eo subtype OMIM:[121360]
About this StructureAbout this Structure
1CL3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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