4j8d: 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=4j8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j8d RCSB], [http://www.ebi.ac.uk/pdbsum/4j8d 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=4j8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j8d RCSB], [http://www.ebi.ac.uk/pdbsum/4j8d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/F10A1_RAT F10A1_RAT]] One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
