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1faf
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| - | [[ | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1faf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Murine_polyomavirus Murine polyomavirus]. 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> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1faf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1faf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1faf RCSB], [http://www.ebi.ac.uk/pdbsum/1faf PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:10950962</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Large T Antigen|Large T Antigen]] | *[[Large T Antigen|Large T Antigen]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Murine polyomavirus]] | [[Category: Murine polyomavirus]] | ||
[[Category: Berjanskii, M V.]] | [[Category: Berjanskii, M V.]] | ||
Revision as of 11:57, 28 September 2014
NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.
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