3esk

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Template:STRUCTURE 3esk

Contents 1 Structure of HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand 2 Function 3 About this Structure 4 Reference

Structure of HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand

Template:ABSTRACT PUBMED 19586912

Function

[STIP1_HUMAN] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB). [HSP7C_HUMAN] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex.^[1]

About this Structure

3esk is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.

Reference

• Kajander T, Sachs JN, Goldman A, Regan L. Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering. J Biol Chem. 2009 Sep 11;284(37):25364-74. Epub 2009 Jul 7. PMID:19586912 doi:10.1074/jbc.M109.033894

1. ↑ Yahata T, de Caestecker MP, Lechleider RJ, Andriole S, Roberts AB, Isselbacher KJ, Shioda T. The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors. J Biol Chem. 2000 Mar 24;275(12):8825-34. PMID:10722728