2f2p: Difference between revisions

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[[Image:2f2p.gif|left|200px]]<br /><applet load="2f2p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2f2p.gif|left|200px]]<br /><applet load="2f2p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2f2p, resolution 2.6Å" />

'''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode'''<br />

==Overview==

Calcineurin is a calmodulin-binding protein in brain and the only, serine/threonine protein phosphatase under the control of Ca2+/calmodulin, (CaM), which plays a critical role in coupling Ca2+ signals to cellular, responses. CaM up-regulates the phosphatase activity of calcineurin by, binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we, report crystal structural studies of CaM bound to a CBD peptide. The, chimeric protein containing CaM and the CBD peptide forms an intimate, homodimer, in which CaM displays a native-like extended conformation and, the CBD peptide shows alpha-helical structure. Unexpectedly, the, N-terminal lobe from one CaM and the C-terminal lobe from the second, molecule form a combined binding site to trap the peptide. Thus, the dimer, provides two binding sites, each of which is reminiscent of the fully, collapsed conformation of CaM commonly observed in complex with, for, example, the myosin light chain kinase (MLCK) peptide. The interaction, between the peptide and CaM is highly specific and similar to MLCK.

Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.

==About this Structure==

2F2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA].

2F2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA].

==Reference==

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[[Category: ef-hands]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:19:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:06 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2f2p.gif|left|200px]]<br /><applet load="2f2p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2f2p.gif|left|200px]]<br /><applet load="2f2p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2f2p, resolution 2.6&Aring;" />
 '''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode'''<br />
 ==Overview==
-Calcineurin is a calmodulin-binding protein in brain and the only, serine/threonine protein phosphatase under the control of Ca2+/calmodulin, (CaM), which plays a critical role in coupling Ca2+ signals to cellular, responses. CaM up-regulates the phosphatase activity of calcineurin by, binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we, report crystal structural studies of CaM bound to a CBD peptide. The, chimeric protein containing CaM and the CBD peptide forms an intimate, homodimer, in which CaM displays a native-like extended conformation and, the CBD peptide shows alpha-helical structure. Unexpectedly, the, N-terminal lobe from one CaM and the C-terminal lobe from the second, molecule form a combined binding site to trap the peptide. Thus, the dimer, provides two binding sites, each of which is reminiscent of the fully, collapsed conformation of CaM commonly observed in complex with, for, example, the myosin light chain kinase (MLCK) peptide. The interaction, between the peptide and CaM is highly specific and similar to MLCK.
+Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.
 ==About this Structure==
-F2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA].
+F2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: ef-hands]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:19:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:06 2008''