4j8e
From Proteopedia
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| - | + | ==Middle domain of Hsc70-interacting protein, crystal form I== | |
| - | + | <StructureSection load='4j8e' size='340' side='right' caption='[[4j8e]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4j8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J8E FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j8c|4j8c]], [[4j8d|4j8d]], [[4j8f|4j8f]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fam10a1, Hip, St13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=4j8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j8e RCSB], [http://www.ebi.ac.uk/pdbsum/4j8e PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Hsp70-interacting protein, Hip, cooperates with the chaperone Hsp70 in protein folding and prevention of aggregation. Hsp70 interacts with non-native protein substrates in an ATP-dependent reaction cycle regulated by J-domain proteins and nucleotide exchange factors (NEFs). Hip is thought to delay substrate release by slowing ADP dissociation from Hsp70. Here we present crystal structures of the dimerization domain and the tetratricopeptide repeat (TPR) domain of rat Hip. As shown in a cocrystal structure, the TPR core of Hip interacts with the Hsp70 ATPase domain through an extensive interface, to form a bracket that locks ADP in the binding cleft. Hip and NEF binding to Hsp70 are mutually exclusive, and thus Hip attenuates active cycling of Hsp70-substrate complexes. This mechanism explains how Hip enhances aggregation prevention by Hsp70 and facilitates transfer of specific proteins to downstream chaperones or the proteasome. | ||
| - | + | Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.,Li Z, Hartl FU, Bracher A Nat Struct Mol Biol. 2013 Aug;20(8):929-35. doi: 10.1038/nsmb.2608. Epub 2013 Jun, 30. PMID:23812373<ref>PMID:23812373</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Bracher, A | + | [[Category: Bracher, A]] |
| - | [[Category: Li, Z | + | [[Category: Li, Z]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Co-chaperone]] | [[Category: Co-chaperone]] | ||
Revision as of 12:49, 21 December 2014
Middle domain of Hsc70-interacting protein, crystal form I
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