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1faf
From Proteopedia
(New page: 200px<br /><applet load="1faf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1faf" /> '''NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF ...) |
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'''NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.'''<br /> | '''NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NMR structure of the N-terminal, DnaJ-like domain of murine | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1FAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murine_polyomavirus Murine polyomavirus]. Full crystallographic information is available from [http:// | + | 1FAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murine_polyomavirus Murine polyomavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Murine polyomavirus]] | [[Category: Murine polyomavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Berjanskii, M | + | [[Category: Berjanskii, M V.]] |
| - | [[Category: Doren, S | + | [[Category: Doren, S R.Van.]] |
| - | [[Category: Folk, W | + | [[Category: Folk, W R.]] |
| - | [[Category: Riley, M | + | [[Category: Riley, M I.]] |
[[Category: Semenchenko, V.]] | [[Category: Semenchenko, V.]] | ||
[[Category: Xie, A.]] | [[Category: Xie, A.]] | ||
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[[Category: j domain]] | [[Category: j domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:38 2008'' |
Revision as of 10:36, 21 February 2008
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NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.
Overview
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.
About this Structure
1FAF is a Single protein structure of sequence from Murine polyomavirus. Full crystallographic information is available from OCA.
Reference
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
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