2ocj

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(New page: 200px<br /> <applet load="2ocj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ocj, resolution 2.050&Aring;" /> '''Human p53 core dom...)
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<applet load="2ocj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2ocj, resolution 2.050&Aring;" />
'''Human p53 core domain in the absence of DNA'''<br />
'''Human p53 core domain in the absence of DNA'''<br />
==Overview==
==Overview==
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The tumor suppressor protein p53 plays a key role in cell-cycle regulation, by triggering DNA repair, cell-cycle arrest and apoptosis when the, appropriate signal is received. p53 has the classic architecture of a, transcription factor, with an amino-terminal transactivation domain, a, core DNA-binding domain and carboxy-terminal tetramerization and, regulatory domains. The crystal structure of the p53 core domain, which, includes the amino acids from residue 96 to residue 289, has been, determined in the absence of DNA to a resolution of 2.05 A. Crystals grew, in a new monoclinic space group (P2(1)), with unit-cell parameters a =, 68.91, b = 69.36, c = 84.18 A, beta = 90.11 degrees . The structure was, solved by molecular replacement and has been refined to a final R factor, of 20.9% (R(free) = 24.6%). The final model contains four molecules in the, asymmetric unit with four zinc ions and 389 water molecules. The, non-crystallographic tetramers display different protein contacts from, those in other p53 crystals, giving rise to the question of how p53, arranges as a tetramer when it binds its target DNA.
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The tumor suppressor protein p53 plays a key role in cell-cycle regulation by triggering DNA repair, cell-cycle arrest and apoptosis when the appropriate signal is received. p53 has the classic architecture of a transcription factor, with an amino-terminal transactivation domain, a core DNA-binding domain and carboxy-terminal tetramerization and regulatory domains. The crystal structure of the p53 core domain, which includes the amino acids from residue 96 to residue 289, has been determined in the absence of DNA to a resolution of 2.05 A. Crystals grew in a new monoclinic space group (P2(1)), with unit-cell parameters a = 68.91, b = 69.36, c = 84.18 A, beta = 90.11 degrees . The structure was solved by molecular replacement and has been refined to a final R factor of 20.9% (R(free) = 24.6%). The final model contains four molecules in the asymmetric unit with four zinc ions and 389 water molecules. The non-crystallographic tetramers display different protein contacts from those in other p53 crystals, giving rise to the question of how p53 arranges as a tetramer when it binds its target DNA.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2OCJ 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OCJ OCA].
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2OCJ 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCJ OCA].
==Reference==
==Reference==
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[[Category: tumor suppressor]]
[[Category: tumor suppressor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:09:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:05 2008''

Revision as of 16:17, 21 February 2008


2ocj, resolution 2.050Å

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Human p53 core domain in the absence of DNA

Contents

Overview

The tumor suppressor protein p53 plays a key role in cell-cycle regulation by triggering DNA repair, cell-cycle arrest and apoptosis when the appropriate signal is received. p53 has the classic architecture of a transcription factor, with an amino-terminal transactivation domain, a core DNA-binding domain and carboxy-terminal tetramerization and regulatory domains. The crystal structure of the p53 core domain, which includes the amino acids from residue 96 to residue 289, has been determined in the absence of DNA to a resolution of 2.05 A. Crystals grew in a new monoclinic space group (P2(1)), with unit-cell parameters a = 68.91, b = 69.36, c = 84.18 A, beta = 90.11 degrees . The structure was solved by molecular replacement and has been refined to a final R factor of 20.9% (R(free) = 24.6%). The final model contains four molecules in the asymmetric unit with four zinc ions and 389 water molecules. The non-crystallographic tetramers display different protein contacts from those in other p53 crystals, giving rise to the question of how p53 arranges as a tetramer when it binds its target DNA.

Disease

Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]

About this Structure

2OCJ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the human p53 core domain in the absence of DNA., Wang Y, Rosengarth A, Luecke H, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):276-81. Epub 2007, Feb 21. PMID:17327663

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