The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
Functional site class:
TPR binding site
Functional site description:
The C-terminal sequence EEVD, which is highly conserved in Hsp70 and Hsp90 protein, bind to the TPR domains.
ELM Description:
Ligands of the TPR (tetratricopeptide repeat motif) domains are EEVD motifs, C-terminal sequences highly conserved in all eukaryotic members of the Hsp70 and Hsp90 families.
Pattern: EEVD$
Pattern Probability: 3.227e-08
Present in taxon: Eukaryota
Interaction Domain:
TPR_1 (PF00515) Tetratricopeptide repeat (Stochiometry: 1 : 1)
PDB Structure: 1ELR
<a href="http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1ELR" title="" target="_blank"><img src="/media/pdb.ico.png"/>1ELR</a>
o See 9 Instances for LIG_TPR
o Abstract
Heat shock proteins (HSPs), also called stress proteins, are a group of proteins that are present in all cells in all life forms. They are induced when a cell undergoes various types of environmental stresses like heat, cold and oxygen deprivation. HSPs are also present in cells under perfectly normal conditions. They act like 'chaperones,' regulating the folding and the conformational regulation of a variety of signal transduction proteins and cell cycle regulators in the eukaryotic cytosol. To achieve the folding of proteins such as steroid hormone receptors and protein kinases, Hsp90 and Hsp70 cooperate with numerous cofactors containing so-called tetratricopeptide repeat (TPR)1 domains. TPR domains are composed of loosely conserved 34-amino acid sequence motifs that are repeated several times per domain. The TPR co-factors of the Hsp70/Hsp90 multi-chaperone system interact with the C-terminal domains of Hsp70 and Hsp90. Deletion mutagenesis suggested that the C-terminal sequence motif EEVD-COOH, which is highly conserved in all Hsp70s and Hsp90s, has an important role in TPR-mediated cofactor binding.
o 3 selected references:

o 6 GO-Terms:

o 9 Instances for LIG_TPR
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
H90A1_DANRE hsp90a.1 722 725 EEDMPVLEGDDDTSRMEEVD TP 2 Danio rerio (Zebrafish)
HSP72_MOUSE Hspa2 630 633 YQGGPGGGGSSGGPTIEEVD TP 2 Mus musculus (House mouse)
HS90A_MOUSE Hsp90aa1 730 733 TEEMPPLEGDDDTSRMEEVD TP 1 Mus musculus (House mouse)
HS90A_HUMAN HSP90AA1 729 732 TEEMPPLEGDDDTSRMEEVD TP 4 Homo sapiens (Human)
HSP72_RAT Hspa2 630 633 YQGGPGGGGSSGGPTIEEVD TP 2 Rattus norvegicus (Norway rat)
HS71L_HUMAN HSPA1L 638 641 CGTGYVPGRPATGPTIEEVD TP 1 Homo sapiens (Human)
HSP72_HUMAN HSPA2 636 639 GGSGGGGSGASGGPTIEEVD TP 4 Homo sapiens (Human)
HSP72_DROME Hsp70Ba 638 641 CGQQAGGFGGYSGPTVEEVD TP 1 Drosophila melanogaster (Fruit fly)
HSP76_PIG HSPA6 640 643 CGAQARQGAPSTGPVIEEVD TP 1 Sus scrofa (Pig)
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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