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New page: left|200px<br /><applet load="1zla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zla, resolution 2.9Å" /> '''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"  
[[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==
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.
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==
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].  
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]]
[[Category: Barbera, A.J.]]
[[Category: Barbera, A J.]]
[[Category: Chodaparambil, J.V.]]
[[Category: Chodaparambil, J V.]]
[[Category: Kaye, K.M.]]
[[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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