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1eoq

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{{STRUCTURE_1eoq| PDB=1eoq | SCENE= }}
{{STRUCTURE_1eoq| PDB=1eoq | SCENE= }}
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'''ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN'''
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===ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN===
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==Overview==
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BACKGROUND: The capsid protein (CA) of retroviruses, such as Rous sarcoma virus (RSV), consists of two independently folded domains. CA functions as part of a polyprotein during particle assembly and budding and, in addition, forms a shell encapsidating the genomic RNA in the mature, infectious virus. RESULTS: The structures of the N- and C-terminal domains of RSV CA have been determined by X-ray crystallography and solution nuclear magnetic resonance (NMR) spectroscopy, respectively. The N-terminal domain comprises seven alpha helices and a short beta hairpin at the N terminus. The N-terminal domain associates through a small, tightly packed, twofold symmetric interface within the crystal, different from those previously described for other retroviral CAs. The C-terminal domain is a compact bundle of four alpha helices, although the last few residues are disordered. In dilute solution, RSV CA is predominantly monomeric. We show, however, using electron microscopy, that intact RSV CA can assemble in vitro to form both tubular structures constructed from toroidal oligomers and planar monolayers. Both modes of assembly occur under similar solution conditions, and both sheets and tubes exhibit long-range order. CONCLUSIONS: The tertiary structure of CA is conserved across the major retroviral genera, yet sequence variations are sufficient to cause change in associative behavior. CA forms the exterior shell of the viral core in all mature retroviruses. However, the core morphology differs between viruses. Consistent with this observation, we find that the capsid proteins of RSV and human immunodeficiency virus type 1 exhibit different associative behavior in dilute solution and assemble in vitro into different structures.
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(as it appears on PubMed at http://www.pubmed.gov), where 10873863 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10873863}}
==About this Structure==
==About this Structure==
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1EOQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOQ OCA].
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1EOQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOQ OCA].
==Reference==
==Reference==
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[[Category: Vogt, V M.]]
[[Category: Vogt, V M.]]
[[Category: Virus/viral protein]]
[[Category: Virus/viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:21:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:21:14 2008''

Revision as of 22:21, 30 June 2008

Image:1eoq.png

Template:STRUCTURE 1eoq

ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN

Template:ABSTRACT PUBMED 10873863

About this Structure

1EOQ is a Single protein structure of sequence from Rous sarcoma virus. Full experimental information is available from OCA.

Reference

Structure and self-association of the Rous sarcoma virus capsid protein., Kingston RL, Fitzon-Ostendorp T, Eisenmesser EZ, Schatz GW, Vogt VM, Post CB, Rossmann MG, Structure. 2000 Jun 15;8(6):617-28. PMID:10873863

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