1zm0

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(New page: 200px<br /> <applet load="1zm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zm0, resolution 2.100&Aring;" /> '''Crystal Structure ...)
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[[Image:1zm0.gif|left|200px]]<br /><applet load="1zm0" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1zm0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1zm0, resolution 2.100&Aring;" />
caption="1zm0, resolution 2.100&Aring;" />
'''Crystal Structure of the Carboxyl Terminal PH Domain of Pleckstrin To 2.1 Angstroms'''<br />
'''Crystal Structure of the Carboxyl Terminal PH Domain of Pleckstrin To 2.1 Angstroms'''<br />
==Overview==
==Overview==
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Pleckstrin is an important intracellular protein involved in the, phosphoinositide-signalling pathways of platelet activation. This protein, contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and, C-PH). The crystal structure of C-PH was solved by molecular replacement, and refined at 2.1 Angstroms resolution. Two molecules were observed, within the asymmetric unit and it is proposed that the resulting dimer, interface could contribute to the previously observed oligomerization of, pleckstrin in resting platelets. Structural comparisons between the, phosphoinositide-binding loops of the C-PH crystal structure and the PH, domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a, recently described solution structure of C-PH are presented and discussed.
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Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1ZM0 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=1ZM0 OCA].
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1ZM0 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=1ZM0 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Haslam, R.J.]]
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[[Category: Haslam, R J.]]
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[[Category: Jackson, S.G.]]
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[[Category: Jackson, S G.]]
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[[Category: Junop, M.S.]]
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[[Category: Junop, M S.]]
[[Category: Summerfield, R.]]
[[Category: Summerfield, R.]]
[[Category: Zhang, K.]]
[[Category: Zhang, K.]]
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[[Category: pleckstrin]]
[[Category: pleckstrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:36:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:53 2008''

Revision as of 14:16, 21 February 2008


1zm0, resolution 2.100Å

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Crystal Structure of the Carboxyl Terminal PH Domain of Pleckstrin To 2.1 Angstroms

Contents

Overview

Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed.

Disease

Known disease associated with this structure: Age-related maculopathy, susceptibility to OMIM:[607772]

About this Structure

1ZM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms., Jackson SG, Zhang Y, Bao X, Zhang K, Summerfield R, Haslam RJ, Junop MS, Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):324-30. Epub 2006, Feb 22. PMID:16510979

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