1co1: Difference between revisions

New page: left|200px<br /> <applet load="1co1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1co1" /> '''FOLD OF THE CBFA'''<br /> ==Overview== BAC...
 
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<applet load="1co1" size="450" color="white" frame="true" align="right" spinBox="true"  
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'''FOLD OF THE CBFA'''<br />
'''FOLD OF THE CBFA'''<br />


==Overview==
==Overview==
BACKGROUND: CBFA is the DNA-binding subunit of the transcription factor, complex called core binding factor, or CBF. Knockout of the Cbfa2 gene in, mice leads to embryonic lethality and a profound block in hematopoietic, development. Chromosomal disruptions of the human CBFA gene are associated, with a large percentage of human leukemias. RESULTS: Utilizing nuclear, magnetic resonance spectroscopy we have determined the three-dimensional, fold of the CBFA Runt domain in its DNA-bound state, showing that it is an, s-type immunoglobulin (Ig) fold. DNA binding by the Runt domain is shown, to be mediated by loop regions located at both ends of the Runt domain Ig, fold. A putative site for CBFB binding has been identified; the spatial, location of this site provides a rationale for the ability of CBFB to, modulate the affinity of the Runt domain for DNA. CONCLUSIONS: Structural, comparisons demonstrate that the s-type Ig fold found in the Runt domain, is conserved in the Ig folds found in the DNA-binding domains of, NF-kappaB, NFAT, p53, STAT-1, and the T-domain. Thus, these proteins form, a family of structurally and functionally related DNA-binding domains., Unlike the other members of this family, the Runt domain utilizes loops at, both ends of the Ig fold for DNA recognition.
BACKGROUND: CBFA is the DNA-binding subunit of the transcription factor complex called core binding factor, or CBF. Knockout of the Cbfa2 gene in mice leads to embryonic lethality and a profound block in hematopoietic development. Chromosomal disruptions of the human CBFA gene are associated with a large percentage of human leukemias. RESULTS: Utilizing nuclear magnetic resonance spectroscopy we have determined the three-dimensional fold of the CBFA Runt domain in its DNA-bound state, showing that it is an s-type immunoglobulin (Ig) fold. DNA binding by the Runt domain is shown to be mediated by loop regions located at both ends of the Runt domain Ig fold. A putative site for CBFB binding has been identified; the spatial location of this site provides a rationale for the ability of CBFB to modulate the affinity of the Runt domain for DNA. CONCLUSIONS: Structural comparisons demonstrate that the s-type Ig fold found in the Runt domain is conserved in the Ig folds found in the DNA-binding domains of NF-kappaB, NFAT, p53, STAT-1, and the T-domain. Thus, these proteins form a family of structurally and functionally related DNA-binding domains. Unlike the other members of this family, the Runt domain utilizes loops at both ends of the Ig fold for DNA recognition.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1CO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CO1 OCA].  
1CO1 is a [http://en.wikipedia.org/wiki/Single_protein 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=1CO1 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berardi, M.J.]]
[[Category: Berardi, M J.]]
[[Category: Bushweller, J.H.]]
[[Category: Bushweller, J H.]]
[[Category: cbfa runt aml-1 runt domain]]
[[Category: cbfa runt aml-1 runt domain]]


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