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4fmm
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmm RCSB], [http://www.ebi.ac.uk/pdbsum/4fmm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmm RCSB], [http://www.ebi.ac.uk/pdbsum/4fmm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PDR16_YEAST PDR16_YEAST]] Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover.<ref>PMID:9890948</ref> <ref>PMID:10848624</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 02:11, 25 December 2014
Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding
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