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ComplexViewer 2.2.1by Rappsilber LaboratoryHIF1AELOCVHLELOBtooltip

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Node Shape
Protein: click to switch
Interaction
EBI-8837467
MI Features
deg_odph_vhl_1
n-terminus
required hydroxypro-402
btb/poz_fold
vhl_tumour_suppress_b/a_dom

Interaction Details

Accession
EBI-8837467
Detection Method
spr
Host Organism
In vitro
Positive Interaction
✔️
External Cross References (1)
DatabaseIdentifier
imex
Annotations (7)
TopicDescription
curation depth imex curation
kinetic_conditions Temp = 25C
accepted Accepted 2013-NOV-29 by PPORRAS
author-announcement 13-Jan-2014: Contacted by IntAct-Help.
figure legend Table 1
data-processing Ranges for the regions of pVHL and elongin C were taken from PMID:10205047.
kinetics Kinetic parameters for binding of Hif1a to VHL-elonginB/C complex were determined for different Hif1a peptides. For Hif1a (residues 390-417): kon = 7.9 +/- 0.07 x 10E+5 M-1 s-1, koff = 4.1 +/- 0.03 x 10E-2 s-1 and Kd = 5.2 x 10E-8 molar. For Hif1a (residues 395-406): kon = 4.9 +/- 0.02 x 10E+5 M-1 s-1, koff = 4.5 +/- 0.01 x 10E-2 s-1 and Kd = 9.3 x 10E-8 molar.
Parameters (3)
TypeUnitValue
kon 7.9000000000000003552713678800500929355621337890625x10^(5)
kd 5.20000000000000017763568394002504646778106689453125x10^(-8)
koff 4.0999999999999996447286321199499070644378662109375x10^(-2)

Publication

Title
Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.
Journal
Nature (0028-0836)
Authors
Hon W.C.,Wilson M.I.,Harlos K.,Claridge T.D.,Schofield C.J.,Pugh C.W.,Maxwell P.H.,Ratcliffe P.J.,Stuart D.I.,Jones E.Y.
Publication date
01/01/2002
Publication reference
PubMed: 12050673
External Cross References (1)
DatabaseIdentifier
imex
Annotations (1)
TopicDescription
contact-email yvonne@strubi.ox.ac.uk,peter.ratcliffe@ndm.ox.ac.uk