1x9p
From Proteopedia
(New page: 200px<br /><applet load="1x9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9p, resolution 3.30Å" /> '''The crystal structur...) |
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| - | [[Image:1x9p.gif|left|200px]]<br /><applet load="1x9p" size=" | + | [[Image:1x9p.gif|left|200px]]<br /><applet load="1x9p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x9p, resolution 3.30Å" /> | caption="1x9p, resolution 3.30Å" /> | ||
'''The crystal structure of human adenovirus 2 penton base'''<br /> | '''The crystal structure of human adenovirus 2 penton base'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The adenovirus penton, a noncovalent complex of the pentameric penton base | + | The adenovirus penton, a noncovalent complex of the pentameric penton base and trimeric fiber proteins, comprises the vertices of the adenovirus capsid and contains all necessary components for viral attachment and internalization. The 3.3 A resolution crystal structure of human adenovirus 2 (hAd2) penton base shows that the monomer has a basal jellyroll domain and a distal irregular domain formed by two long insertions, a similar topology to the adenovirus hexon. The Arg-Gly-Asp (RGD) motif, required for interactions with cellular integrins, occurs on a flexible surface loop. The complex of penton base with bound N-terminal fiber peptide, determined at 3.5 A resolution, shows that the universal fiber motif FNPVYPY binds at the interface of adjacent penton base monomers and results in a localized structural rearrangement in the insertion domain of the penton base. These results give insight into the structure and assembly of the adenovirus capsid and will be of use for gene-therapy applications. |
==About this Structure== | ==About this Structure== | ||
| - | 1X9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2] with SO4 and C15 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1X9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=C15:'>C15</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: jellyroll domain]] | [[Category: jellyroll domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:28 2008'' |
Revision as of 13:52, 21 February 2008
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The crystal structure of human adenovirus 2 penton base
Overview
The adenovirus penton, a noncovalent complex of the pentameric penton base and trimeric fiber proteins, comprises the vertices of the adenovirus capsid and contains all necessary components for viral attachment and internalization. The 3.3 A resolution crystal structure of human adenovirus 2 (hAd2) penton base shows that the monomer has a basal jellyroll domain and a distal irregular domain formed by two long insertions, a similar topology to the adenovirus hexon. The Arg-Gly-Asp (RGD) motif, required for interactions with cellular integrins, occurs on a flexible surface loop. The complex of penton base with bound N-terminal fiber peptide, determined at 3.5 A resolution, shows that the universal fiber motif FNPVYPY binds at the interface of adjacent penton base monomers and results in a localized structural rearrangement in the insertion domain of the penton base. These results give insight into the structure and assembly of the adenovirus capsid and will be of use for gene-therapy applications.
About this Structure
1X9P is a Single protein structure of sequence from Human adenovirus 2 with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of the human adenovirus 2 penton., Zubieta C, Schoehn G, Chroboczek J, Cusack S, Mol Cell. 2005 Jan 7;17(1):121-35. PMID:15629723
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