SASDAX4: uPAR wild-type ATF complex (Urokinase plasminogen activator surfa...

Basic information

Entry

Database: SASBDB / ID: SASDAX4

Sample

uPAR wild-type ATF complex

• Urokinase plasminogen activator surface receptor (protein), uPAR, Homo sapiens
• Urokinase-type plasminogen activator (protein), ATF, Homo sapiens

Function / homology

Function:

urokinase plasminogen activator receptor activity / Attachment of GPI anchor to uPAR / positive regulation of homotypic cell-cell adhesion / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of signaling receptor activity / regulation of smooth muscle cell migration / serine-type endopeptidase complex / Dissolution of Fibrin Clot / extrinsic component of membrane / smooth muscle cell migration / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of DNA binding / plasminogen activation / negative regulation of intrinsic apoptotic signaling pathway / regulation of cell adhesion mediated by integrin / positive regulation of release of cytochrome c from mitochondria / tertiary granule membrane / regulation of proteolysis / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / serine protease inhibitor complex / fibrinolysis / cell projection / chemotaxis / blood coagulation / signaling receptor activity / regulation of cell population proliferation / positive regulation of protein phosphorylation / response to hypoxia / positive regulation of cell migration / protein domain specific binding / endoplasmic reticulum lumen / external side of plasma membrane / signaling receptor binding / serine-type endopeptidase activity / focal adhesion / Neutrophil degranulation / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane

Domain/homology:

CD59 antigen, conserved site / Ly-6 / u-PAR domain signature. / u-PAR/Ly-6 domain / Ly-6 antigen / uPA receptor -like domain / Ly-6 antigen/uPA receptor-like / Snake toxin-like superfamily / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / : / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan

Component:

Urokinase-type plasminogen activator / Urokinase plasminogen activator surface receptor

• Biological species: Homo sapiens (human)
• Citation: Journal: J Biol Chem / Year: 2012; Title: A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR).; Authors: Haydyn D T Mertens / Magnus Kjaergaard / Simon Mysling / Henrik Gårdsvoll / Thomas J D Jørgensen / Dmitri I Svergun / Michael Ploug / ; Abstract: The urokinase-type plasminogen activator receptor (uPAR) provides a rendezvous between proteolytic degradation of the extracellular matrix and integrin-mediated adhesion to vitronectin. These processes are, however, tightly linked because the high affinity binding of urokinase regulates the binding of uPAR to matrix-embedded vitronectin. Although crystal structures exist to define the corresponding static bi- and trimolecular receptor complexes, it is evident that the dynamic property of uPAR plays a decisive role in its function. In the present study, we combine small angle x-ray scattering, hydrogen-deuterium exchange, and surface plasmon resonance to develop a structural model describing the allosteric regulation of uPAR. We show that the flexibility of its N-terminal domain provides the key for understanding this allosteric mechanism. Importantly, our model has direct implications for understanding uPAR-assisted cell adhesion and migration as well as for translational research, including targeted intervention therapy and non-invasive tumor imaging in vivo.

Contact author

• Haydyn Mertens (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

Models

Sample

• Sample: Name: uPAR wild-type ATF complex / Sample MW: 85.49 kDa / Specimen concentration: 1.50-4.40 / Concentration method: A280 / Entity id: 66 / 67
• Buffer: Name: Sodium Phosphate / Concentration: 25.00 mM / pH: 7.2 / Composition: Glycerol 5.000 %, NaSO4 50.000 mM

Entity #66

Name: uPAR / Type: protein
Description: Urokinase plasminogen activator surface receptor
Formula weight: 36.98 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q03405
Sequence:

MGHPPLLPLL LLLHTCVPAS WGLRCMQCKT NGDCRVEECA LGQDLCRTTI VRLWEEGEEL ELVEKSCTHS EKTNRTLSYR TGLKITSLTE VVCGLDLCNQ GNSGRAVTYS RSRYLECISC GSSDMSCERG RHQSLQCRSP EEQCLDVVTH WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG FHNNDTFHFL KCCNTTKCNE GPILELENLP QNGRQCYSCK GNSTHGCSSE ETFLIDCRGP MNQCLVATGT HEPKNQSYMV RGCATASMCQ HAHLGDAFSM NHIDVSCCTK SGCNHPDLDV QYRSGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT

Entity #67

Name: ATF / Type: protein / Description: Urokinase-type plasminogen activator / Formula weight: 48.51 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P00749
Sequence:

MRALLARLLL CVLVVSDSKG SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSHFLPWIR SHTKEENGLA L

Experimental information

• Beam: Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
• Detector: Name: Pilatus 1M-W / Pixsize x: 0.172 mm

Scan

Title: uPAR wild-type ATF complex / Measurement date: Jun 10, 2010 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 30 sec. / Number of frames: 4 / Unit: 1/nm /

	Min	Max
Q	0.0675	6.3452

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 374 /

	Min	Max
Q	0.2191	2.224
P(R) point	57	430
R	0	9.38

Result

Type of curve: merged / Standard: BSA /

	Experimental	Standard	Porod
MW	58 kDa	58 kDa	-
Volume	-	-	102 nm3

	Guinier	P(R)
Forward scattering, I0	62.3	-
Radius of gyration, Rg	2.8 nm	2.8 nm

	Min	Max
D	-	9.4
Guinier point	57	149