We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1faf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:11, 19 June 2019

NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.

Structural highlights

1faf is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LT_POVM3] Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription (By similarity).

Publication Abstract from PubMed

The NMR structure of the N-terminal, DnaJ-like domain of murine polyomavirus tumor antigens (PyJ) has been determined to high precision, with root mean square deviations to the mean structure of 0.38 A for backbone atoms and 0.94 A for all heavy atoms of ordered residues 5-41 and 50-69. PyJ possesses a three-helix fold, in which anti-parallel helices II and III are bridged by helix I, similar to the four-helix fold of the J domains of DnaJ and human DnaJ-1. PyJ differs significantly in the lengths of N terminus, helix I, and helix III. The universally conserved HPD motif appears to form a His-Pro C-cap of helix II. Helix I features a stabilizing Schellman C-cap that is probably conserved universally among J domains. On the helix II surface where positive charges of other J domains have been implicated in binding of hsp70s, PyJ contains glutamine residues. Nonetheless, chimeras that replace the J domain of DnaJ with PyJ function like wild-type DnaJ in promoting growth of Escherichia coli. This activity can be modulated by mutations of at least one of these glutamines. T antigen mutations reported to impair cellular transformation by the virus, presumably via interactions with PP2A, cluster in the hydrophobic folding core and at the extreme N terminus, remote from the HPD loop.

NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens.,Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR J Biol Chem. 2000 Nov 17;275(46):36094-103. PMID:10950962^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR. NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens. J Biol Chem. 2000 Nov 17;275(46):36094-103. PMID:10950962 doi:10.1074/jbc.M006572200

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1faf"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.==
-<StructureSection load='1faf' size='340' side='right' caption='[[1faf]], [[NMR_Ensembles_of_Models | 47 NMR models]]' scene=''>
+<StructureSection load='1faf' size='340' side='right'caption='[[1faf]], [[NMR_Ensembles_of_Models | 47 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1faf]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FAF FirstGlance]. <br>
@@ Line 24: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Berjanskii, M V]]
 [[Category: Doren, S R.Van]]

1faf

From Proteopedia

Revision as of 07:11, 19 June 2019

NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox