1u7k
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(New page: 200px<br /><applet load="1u7k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7k, resolution 1.85Å" /> '''Structure of a hexam...)
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Revision as of 01:46, 21 November 2007
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Structure of a hexameric N-terminal domain from murine leukemia virus capsid
Overview
Retroviruses are the aetiological agents of a range of human diseases, including AIDS and T-cell leukaemias. They follow complex life cycles, which are still only partly understood at the molecular level. Maturation, of newly formed retroviral particles is an essential step in production of, infectious virions, and requires proteolytic cleavage of Gag polyproteins, in the immature particle to form the matrix, capsid and nucleocapsid, proteins present in the mature virion. Capsid proteins associate to form a, dense viral core that may be spherical, cylindrical or conical depending, on the genus of the virus. Nonetheless, these assemblies all appear to be, composed of a lattice formed from hexagonal rings, each containing six, capsid monomers. Here, we describe the X-ray structure of an individual, hexagonal assembly from N-tropic murine leukaemia virus (N-MLV). The, interface between capsid monomers is generally polar, consistent with weak, interactions within the hexamer. Similar architectures are probably, crucial for the regulation of capsid assembly and disassembly in all, retroviruses. Together, these observations provide new insights into, retroviral uncoating and how cellular restriction factors may interfere, with viral replication.
About this Structure
1U7K is a Single protein structure of sequence from Viruses. Full crystallographic information is available from OCA.
Reference
High-resolution structure of a retroviral capsid hexameric amino-terminal domain., Mortuza GB, Haire LF, Stevens A, Smerdon SJ, Stoye JP, Taylor IA, Nature. 2004 Sep 23;431(7007):481-5. PMID:15386017
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