1zla

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(New page: 200px<br /><applet load="1zla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zla, resolution 2.9&Aring;" /> '''X-ray Structure of a ...)
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[[Image:1zla.gif|left|200px]]<br /><applet load="1zla" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zla.gif|left|200px]]<br /><applet load="1zla" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zla, resolution 2.9&Aring;" />
caption="1zla, resolution 2.9&Aring;" />
'''X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core'''<br />
'''X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core'''<br />
==Overview==
==Overview==
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Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear, antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We, find that N-terminal LANA docks onto chromosomes by binding nucleosomes, through the folded region of histones H2A-H2B. The same LANA residues were, required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B;, chromatin binding was rescued after assembly of nucleosomes containing, H2A-H2B. We also describe the 2.9-angstrom crystal structure of a, nucleosome complexed with the first 23 LANA amino acids. The LANA peptide, forms a hairpin that interacts exclusively with an acidic H2A-H2B region, that is implicated in the formation of higher order chromatin structure., Our findings present a paradigm for how nucleosomes may serve as binding, platforms for viral and cellular proteins and reveal a previously unknown, mechanism for KSHV latency.
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Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We find that N-terminal LANA docks onto chromosomes by binding nucleosomes through the folded region of histones H2A-H2B. The same LANA residues were required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B; chromatin binding was rescued after assembly of nucleosomes containing H2A-H2B. We also describe the 2.9-angstrom crystal structure of a nucleosome complexed with the first 23 LANA amino acids. The LANA peptide forms a hairpin that interacts exclusively with an acidic H2A-H2B region that is implicated in the formation of higher order chromatin structure. Our findings present a paradigm for how nucleosomes may serve as binding platforms for viral and cellular proteins and reveal a previously unknown mechanism for KSHV latency.
==About this Structure==
==About this Structure==
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1ZLA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Expression_vector_pcy215 Expression vector pcy215], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZLA OCA].
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1ZLA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Expression_vector_pcy215 Expression vector pcy215], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLA OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Barbera, A.J.]]
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[[Category: Barbera, A J.]]
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[[Category: Chodaparambil, J.V.]]
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[[Category: Chodaparambil, J V.]]
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[[Category: Kaye, K.M.]]
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[[Category: Kaye, K M.]]
[[Category: Luger, K.]]
[[Category: Luger, K.]]
[[Category: chromatin]]
[[Category: chromatin]]
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[[Category: protein/protein interaction]]
[[Category: protein/protein interaction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:31:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:40 2008''

Revision as of 14:16, 21 February 2008


1zla, resolution 2.9Å

Drag the structure with the mouse to rotate

X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core

Overview

Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We find that N-terminal LANA docks onto chromosomes by binding nucleosomes through the folded region of histones H2A-H2B. The same LANA residues were required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B; chromatin binding was rescued after assembly of nucleosomes containing H2A-H2B. We also describe the 2.9-angstrom crystal structure of a nucleosome complexed with the first 23 LANA amino acids. The LANA peptide forms a hairpin that interacts exclusively with an acidic H2A-H2B region that is implicated in the formation of higher order chromatin structure. Our findings present a paradigm for how nucleosomes may serve as binding platforms for viral and cellular proteins and reveal a previously unknown mechanism for KSHV latency.

About this Structure

1ZLA is a Protein complex structure of sequences from Expression vector pcy215, Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA.

Reference

The nucleosomal surface as a docking station for Kaposi's sarcoma herpesvirus LANA., Barbera AJ, Chodaparambil JV, Kelley-Clarke B, Joukov V, Walter JC, Luger K, Kaye KM, Science. 2006 Feb 10;311(5762):856-61. PMID:16469929

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