1p8x

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(New page: 200px<br /> <applet load="1p8x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p8x, resolution 2.0&Aring;" /> '''The Calcium-Activate...)
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'''The Calcium-Activated C-terminal half of gelsolin'''<br />
'''The Calcium-Activated C-terminal half of gelsolin'''<br />
==Overview==
==Overview==
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Gelsolin requires activation to carry out its severing and capping, activities on F-actin. Here, we present the structure of the isolated, C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of, Ca(2+) ions. This structure completes a triptych of the states of, activation of G4-G6 that illuminates its role in the function of gelsolin., Activated G4-G6 displays an open conformation, with the actin-binding site, on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither, actin nor the type-l Ca(2+), which normally is sandwiched between actin, and G4, is required to achieve this conformation.
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Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1P8X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1P8X OCA].
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1P8X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1P8X OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Burtnick, L.D.]]
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[[Category: Burtnick, L D.]]
[[Category: Narayan, K.]]
[[Category: Narayan, K.]]
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[[Category: Robinson, R.C.]]
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[[Category: Robinson, R C.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-binding]]
[[Category: calcium-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:41:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:24 2008''

Revision as of 12:26, 21 February 2008


1p8x, resolution 2.0Å

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The Calcium-Activated C-terminal half of gelsolin

Contents

Overview

Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.

Disease

Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]

About this Structure

1P8X is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin., Narayan K, Chumnarnsilpa S, Choe H, Irobi E, Urosev D, Lindberg U, Schutt CE, Burtnick LD, Robinson RC, FEBS Lett. 2003 Sep 25;552(2-3):82-5. PMID:14527664

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