1k1f: Difference between revisions

Line 1:

[[Image:1k1f.gif|left|200px]]<br />

[[Image:1k1f.gif|left|200px]]<br /><applet load="1k1f" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1k1f" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1k1f, resolution 2.20Å" />

'''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''<br />

==Overview==

The Bcr-Abl oncoprotein is responsible for a wide range of human, leukemias, including most cases of Philadelphia chromosome-positive, chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for, oncogenicity. We determined the crystal structure of the N-terminal, oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a, novel mode of oligomer formation. Two N-shaped monomers dimerize by, swapping N-terminal helices and by forming an antiparallel coiled coil, between C-terminal helices. Two dimers then stack onto each other to form, a tetramer. The Bcr1-72 structure provides a basis for the design of, inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl, oligomerization.

The Bcr-Abl oncoprotein is responsible for a wide range of human leukemias, including most cases of Philadelphia chromosome-positive chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for oncogenicity. We determined the crystal structure of the N-terminal oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a novel mode of oligomer formation. Two N-shaped monomers dimerize by swapping N-terminal helices and by forming an antiparallel coiled coil between C-terminal helices. Two dimers then stack onto each other to form a tetramer. The Bcr1-72 structure provides a basis for the design of inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl oligomerization.

==Disease==

Line 11:

Line 10:

==About this Structure==

1K1F 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=1K1F OCA].

1K1F 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=1K1F OCA].

==Reference==

Line 18:

Line 17:

[[Category: Single protein]]

[[Category: Ghaffari, S.]]

[[Category: Kim, P.S.]]

[[Category: Kim, P S.]]

[[Category: Lodish, H.]]

[[Category: Malashkevich, V.N.]]

[[Category: Malashkevich, V N.]]

[[Category: Zhao, X.]]

[[Category: bcr-abl kinase]]

Line 26:

Line 25:

[[Category: oligomerization]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:46:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:13 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1k1f.gif|left|200px]]<br />
+[[Image:1k1f.gif|left|200px]]<br /><applet load="1k1f" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1k1f" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1k1f, resolution 2.20&Aring;" />
 '''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''<br />
 ==Overview==
-The Bcr-Abl oncoprotein is responsible for a wide range of human, leukemias, including most cases of Philadelphia chromosome-positive, chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for, oncogenicity. We determined the crystal structure of the N-terminal, oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a, novel mode of oligomer formation. Two N-shaped monomers dimerize by, swapping N-terminal helices and by forming an antiparallel coiled coil, between C-terminal helices. Two dimers then stack onto each other to form, a tetramer. The Bcr1-72 structure provides a basis for the design of, inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl, oligomerization.
+The Bcr-Abl oncoprotein is responsible for a wide range of human leukemias, including most cases of Philadelphia chromosome-positive chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for oncogenicity. We determined the crystal structure of the N-terminal oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a novel mode of oligomer formation. Two N-shaped monomers dimerize by swapping N-terminal helices and by forming an antiparallel coiled coil between C-terminal helices. Two dimers then stack onto each other to form a tetramer. The Bcr1-72 structure provides a basis for the design of inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl oligomerization.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-K1F 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=1K1F OCA].
+K1F 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=1K1F OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Ghaffari, S.]]
-[[Category: Kim, P.S.]]
+[[Category: Kim, P S.]]
 [[Category: Lodish, H.]]
-[[Category: Malashkevich, V.N.]]
+[[Category: Malashkevich, V N.]]
 [[Category: Zhao, X.]]
 [[Category: bcr-abl kinase]]
@@ Line 26: / Line 25: @@
 [[Category: oligomerization]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:46:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:13 2008''