Browse by ORGANISM: Homo sapiens (Human)

SASDUU7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound FCER1G diphospho-ITAM peptide

Tyrosine-protein kinase SYKHigh affinity immunoglobulin epsilon receptor subunit gamma experimental SAS data
Tyrosine-protein kinase SYK High affinity immunoglobulin epsilon receptor subunit gamma Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
High affinity immunoglobulin epsilon receptor subunit gamma monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 54 nm3

SASDUV7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound CD3G diphospho-ITAM peptide

Tyrosine-protein kinase SYKT-cell surface glycoprotein CD3 gamma chain experimental SAS data
Tyrosine-protein kinase SYK T-cell surface glycoprotein CD3 gamma chain Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
T-cell surface glycoprotein CD3 gamma chain monomer, 3 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 56 nm3

SASDUW7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound TYROBP diphospho-ITAM peptide

Tyrosine-protein kinase SYKTYRO protein tyrosine kinase-binding protein experimental SAS data
Tyrosine-protein kinase SYK TYRO protein tyrosine kinase-binding protein Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
TYRO protein tyrosine kinase-binding protein monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 53 nm3

SASDNW9 – Glucose-regulated protein 78, nucleotide-binding domain

Endoplasmic reticulum chaperone BiP experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Endoplasmic reticulum chaperone BiP monomer, 42 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 21
Structural basis of CDNF interaction with the UPR regulator GRP78. Nat Commun 15(1):8175 (2024)
Graewert MA, Volkova M, Jonasson K, Määttä JAE, Gräwert T, Mamidi S, Kulesskaya N, Evenäs J, Johnsson RE, Svergun D, Bhattacharjee A, Huttunen HJ
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 70 nm3

SASDNX9 – Glucose-regulated protein 78 nucleotide-binding domain (GRP78-NBD) in complex with Cerebral dopamine neurotrophic factor (CDNF)

Endoplasmic reticulum chaperone BiPCerebral dopamine neurotrophic factor experimental SAS data
SREFLEX model
Sample: Endoplasmic reticulum chaperone BiP monomer, 42 kDa Homo sapiens protein
Cerebral dopamine neurotrophic factor monomer, 21 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 21
Structural basis of CDNF interaction with the UPR regulator GRP78. Nat Commun 15(1):8175 (2024)
Graewert MA, Volkova M, Jonasson K, Määttä JAE, Gräwert T, Mamidi S, Kulesskaya N, Evenäs J, Johnsson RE, Svergun D, Bhattacharjee A, Huttunen HJ
RgGuinier 2.8 nm
Dmax 10.0 nm
VolumePorod 75 nm3

SASDQS6 – Glucose-regulated protein 78 nucleotide-binding domain (GRP78-NBD) in complex with the C-terminal of Cerebral dopamine neurotrophic factor (C-CDNF)

Endoplasmic reticulum chaperone BiPC-terminal of the Cerebral dopamine neurotrophic factor experimental SAS data
SREFLEX model
Sample: Endoplasmic reticulum chaperone BiP monomer, 42 kDa Homo sapiens protein
C-terminal of the Cerebral dopamine neurotrophic factor monomer, 7 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 23
Structural basis of CDNF interaction with the UPR regulator GRP78. Nat Commun 15(1):8175 (2024)
Graewert MA, Volkova M, Jonasson K, Määttä JAE, Gräwert T, Mamidi S, Kulesskaya N, Evenäs J, Johnsson RE, Svergun D, Bhattacharjee A, Huttunen HJ
RgGuinier 2.4 nm
Dmax 6.9 nm
VolumePorod 66 nm3

SASDUQ4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) WT hub domain

Calcium/calmodulin-dependent protein kinase type II subunit alpha experimental SAS data
PYMOL model
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha dodecamer, 186 kDa Homo sapiens protein
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Oct 3
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.5 nm
Dmax 15.2 nm
VolumePorod 367 nm3

SASDUR4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) WT hub domain

Calcium/calmodulin-dependent protein kinase type II subunit alpha experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha dodecamer, 186 kDa Homo sapiens protein
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2020 Nov 19
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.4 nm
Dmax 14.9 nm
VolumePorod 351 nm3

SASDUS4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) WT hub domain with PIPA (i)

Calcium/calmodulin-dependent protein kinase type II subunit alpha2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid experimental SAS data
PYMOL model
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha dodecamer, 186 kDa Homo sapiens protein
2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 200 µM PIPA, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2022 Nov 30
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.8 nm
Dmax 16.0 nm
VolumePorod 396 nm3

SASDUT4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) WT hub domain with PIPA (ii)

Calcium/calmodulin-dependent protein kinase type II subunit alpha2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid experimental SAS data
PYMOL model
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha dodecamer, 186 kDa Homo sapiens protein
2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 200 µM PIPA, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2023 May 30
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 5.5 nm
Dmax 27.0 nm