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: 1ELW
<a href="http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1ELW" title="" target="_blank"><img src="/media/pdb.ico.png"/>1ELW</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)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
Q90474 hsp90a.1
H90A1_DANRE
722 725 EEDMPVLEGDDDTSRMEEVD TP 2 Danio rerio (Zebrafish)
P17156 Hspa2
HSP72_MOUSE
630 633 YQGGPGGGGSSGGPTIEEVD TP 2 Mus musculus (House mouse)
P07901 Hsp90aa1
HS90A_MOUSE
730 733 TEEMPPLEGDDDTSRMEEVD TP 1 Mus musculus (House mouse)
P07900 HSP90AA1
HS90A_HUMAN
729 732 TEEMPPLEGDDDTSRMEEVD TP 4 Homo sapiens (Human)
P14659 Hspa2
HSP72_RAT
630 633 YQGGPGGGGSSGGPTIEEVD TP 2 Rattus norvegicus (Norway rat)
P34931 HSPA1L
HS71L_HUMAN
638 641 CGTGYVPGRPATGPTIEEVD TP 1 Homo sapiens (Human)
P54652 HSPA2
HSP72_HUMAN
636 639 GGSGGGGSGASGGPTIEEVD TP 4 Homo sapiens (Human)
Q8INI8 Hsp70Ba
HSP72_DROME
638 641 CGQQAGGFGGYSGPTVEEVD TP 1 Drosophila melanogaster (Fruit fly)
Q04967 HSPA6
HSP76_PIG
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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