1prw

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(New page: 200px<br /><applet load="1prw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prw, resolution 1.70&Aring;" /> '''Crystal structure of...)
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[[Image:1prw.jpg|left|200px]]<br /><applet load="1prw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1prw.jpg|left|200px]]<br /><applet load="1prw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1prw, resolution 1.70&Aring;" />
caption="1prw, resolution 1.70&Aring;" />
'''Crystal structure of bovine brain Ca++ calmodulin in a compact form'''<br />
'''Crystal structure of bovine brain Ca++ calmodulin in a compact form'''<br />
==Overview==
==Overview==
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Calmodulin has been a subject of intense scrutiny since its discovery, because of its unusual properties in regulating the functions of about 100, diverse target enzymes and structural proteins. The original and to date, only crystal conformation of native eukaryotic Ca(2+)-calmodulin, (Ca(2+)-CaM) is a very extended molecule with two widely separated, globular domains linked by an exposed long helix. Here we report the 1.7 A, X-ray structure of a new native Ca(2+)-CaM that is in a compact, ellipsoidal conformation and shows a sharp bend in the linker helix and a, more contracted N-terminal domain. This conformation may offer advantages, for recognition of kinase-type calmodulin targets or small organic, molecule drugs.
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Calmodulin has been a subject of intense scrutiny since its discovery because of its unusual properties in regulating the functions of about 100 diverse target enzymes and structural proteins. The original and to date only crystal conformation of native eukaryotic Ca(2+)-calmodulin (Ca(2+)-CaM) is a very extended molecule with two widely separated globular domains linked by an exposed long helix. Here we report the 1.7 A X-ray structure of a new native Ca(2+)-CaM that is in a compact ellipsoidal conformation and shows a sharp bend in the linker helix and a more contracted N-terminal domain. This conformation may offer advantages for recognition of kinase-type calmodulin targets or small organic molecule drugs.
==About this Structure==
==About this Structure==
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1PRW 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 and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRW OCA].
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1PRW 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> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRW OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fallon, J.L.]]
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[[Category: Fallon, J L.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CA]]
[[Category: CA]]
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[[Category: kinase activator]]
[[Category: kinase activator]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:04:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:54 2008''

Revision as of 12:31, 21 February 2008


1prw, resolution 1.70Å

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Crystal structure of bovine brain Ca++ calmodulin in a compact form

Overview

Calmodulin has been a subject of intense scrutiny since its discovery because of its unusual properties in regulating the functions of about 100 diverse target enzymes and structural proteins. The original and to date only crystal conformation of native eukaryotic Ca(2+)-calmodulin (Ca(2+)-CaM) is a very extended molecule with two widely separated globular domains linked by an exposed long helix. Here we report the 1.7 A X-ray structure of a new native Ca(2+)-CaM that is in a compact ellipsoidal conformation and shows a sharp bend in the linker helix and a more contracted N-terminal domain. This conformation may offer advantages for recognition of kinase-type calmodulin targets or small organic molecule drugs.

About this Structure

1PRW is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

A closed compact structure of native Ca(2+)-calmodulin., Fallon JL, Quiocho FA, Structure. 2003 Oct;11(10):1303-7. PMID:14527397

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