Interaction Details


Details of experiments between Q92743 and P60484
Note that the results of all experiments are listed, regardless of the modification states of the fragments.


Experiment series 1

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKV
Measured dissociation constant (10-6M): 45.13
Standard deviation of dissociation constant (10-6M): 3.48
Experiment method: competitive FP
Details of affinity fitting: Competitive binding equation in ProFit
Number of measurements: 3
Measured pKd: 4.35
PUBMED ID: 36115835

Experiment series 2

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 394-403
Site: PBM
Sequence: EDQHTQITKV
Construct: Biotin-ado-ado-EDQHTQITKV
Average holdup BI: 0.21
Normalized holdup BI: 0.27
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 4.34
PUBMED ID: 36115835
Experimental Details

Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality. Not reported internal standards of holdup layout #6

Experiment series 3

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKV
Average holdup BI: 0.41
Immobilized partner concentration (10-6M): 36
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
Measured pKd: 4.3
PUBMED ID: 36115835

Experiment series 4

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 391-403
Site: PBM
Sequence: EDQHTQITKV
Construct: Biotin-ttds-PFDEDQHTQITKV
Average holdup BI: 0.24
Immobilized partner concentration (10-6M): 17
Experiment method: CALIP_holdup
Details of affinity fitting: lysozyme internal standard
Number of measurements: 1
Measured pKd: 4.28
PUBMED ID: 33382810

Experiment series 5

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKV
Average holdup BI: 0.17
Normalized holdup BI: 0.25
Immobilized partner concentration (10-6M): 19
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 4.27
PUBMED ID: 36115835

Experiment series 6

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Average holdup BI: 0.53
Normalized holdup BI: 0.64
Immobilized partner concentration (10-6M): 17
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 5.08
Experimental Details

not reported internal standards of holdup layout #5

Experiment series 7

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Average holdup BI: 0.52
Normalized holdup BI: 0.65
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 5.08
PUBMED ID: 36115835
Experimental Details

not reported internal standards of holdup layout #6

Experiment series 8

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Average holdup BI: 0.43
Normalized holdup BI: 0.61
Immobilized partner concentration (10-6M): 17
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 5.03
PUBMED ID: 36115835

Experiment series 9

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Measured dissociation constant (10-6M): 10.15
Standard deviation of dissociation constant (10-6M): 0.61
Experiment method: competitive FP
Details of affinity fitting: Competitive binding equation in ProFit
Number of measurements: 3
Measured pKd: 4.99
PUBMED ID: 36115835

Experiment series 10

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Average holdup BI: 0.71
Immobilized partner concentration (10-6M): 29
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
Measured pKd: 4.98
PUBMED ID: 36115835

Experiment series 11

Protein A

Protein: HTRA1
Fragment: 365-480
Site: PDZ
Construct: his6-MBP-TEVsite-PDZ

Protein B

Protein: PTEN
Fragment: 393-403
Site: PBM
Modification: (ALY)402
Sequence: EDQHTQITKV
Construct: biotin-ttds-DEDQHTQITKacV
Average holdup BI: 0.43
Normalized holdup BI: 0.56
Immobilized partner concentration (10-6M): 17
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 4.94
Experimental Details

not reported internal standards of holdup layout #5