1ddb: Difference between revisions

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[[Image:1ddb.gif|left|200px]]<br /><applet load="1ddb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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

caption="1ddb" />

'''STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES'''<br />

==Overview==

Members of the BCL2 family of proteins are key regulators of programmed, cell death, acting either as apoptotic agonists or antagonists. Here we, describe the solution structure of BID, presenting the structure of a, proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2, family members allows us to define a structural superfamily, which has, implications for general mechanisms for regulating proapoptotic activity., It appears two criteria must be met for proapoptotic function within the, BCL2 family: targeting of molecules to intracellular membranes, and, exposure of the BH3 death domain. BID's activity is regulated by a Caspase, 8-mediated cleavage event, exposing the BH3 domain and significantly, changing the surface charge and hydrophobicity, resulting in a change of, cellular localization.

Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization.

==About this Structure==

1DDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA].

1DDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA].

==Reference==

Line 15:

[[Category: Cowburn, D.]]

[[Category: Fushman, D.]]

[[Category: Korsmeyer, S.J.]]

[[Category: Korsmeyer, S J.]]

[[Category: Mcdonnell, J.M.]]

[[Category: Mcdonnell, J M.]]

[[Category: Milliman, C.]]

[[Category: apoptosis]]

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[[Category: programmed cell death]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:11:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ddb.gif|left|200px]]<br /><applet load="1ddb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ddb.gif|left|200px]]<br /><applet load="1ddb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ddb" />
 '''STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES'''<br />
 ==Overview==
-Members of the BCL2 family of proteins are key regulators of programmed, cell death, acting either as apoptotic agonists or antagonists. Here we, describe the solution structure of BID, presenting the structure of a, proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2, family members allows us to define a structural superfamily, which has, implications for general mechanisms for regulating proapoptotic activity., It appears two criteria must be met for proapoptotic function within the, BCL2 family: targeting of molecules to intracellular membranes, and, exposure of the BH3 death domain. BID's activity is regulated by a Caspase, 8-mediated cleavage event, exposing the BH3 domain and significantly, changing the surface charge and hydrophobicity, resulting in a change of, cellular localization.
+Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization.
 ==About this Structure==
-DDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA].
+DDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDB OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Cowburn, D.]]
 [[Category: Fushman, D.]]
-[[Category: Korsmeyer, S.J.]]
+[[Category: Korsmeyer, S J.]]
-[[Category: Mcdonnell, J.M.]]
+[[Category: Mcdonnell, J M.]]
 [[Category: Milliman, C.]]
 [[Category: apoptosis]]
@@ Line 23: / Line 23: @@
 [[Category: programmed cell death]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:11:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:28 2008''