SASDF22: Ternary complex of FcRn ectodomain, FcRn binding optimised human ...

Basic information

Entry

Database: SASBDB / ID: SASDF22

Sample

Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the human growth hormone derivative somapacitan.

• somapacitan (protein), Homo sapiens
• FcRn binding optimised human serum albumin V418M, T420A, E505G, V547A (protein), HSAopt, Homo sapiens
• neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag (protein), FcRn ECD beta, Homo sapiens
• neonatal Fc receptor ectodomain alpha-chain (protein), FcRn ECD alpha, Homo sapiens

Function / homology

Function:

growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / IgG immunoglobulin transcytosis in epithelial cells mediated by FcRn immunoglobulin receptor / animal organ development / regulation of glutamate receptor signaling pathway / regulation of calcium ion import across plasma membrane / aspartic-type endopeptidase inhibitor activity / glycosaminoglycan binding / positive regulation of multicellular organism growth / Ciprofloxacin ADME / exogenous protein binding / cellular response to calcium ion starvation / growth hormone receptor binding / positive regulation of D-glucose transmembrane transport / type 5 metabotropic glutamate receptor binding / negative regulation of interleukin-17 production / negative regulation of dendritic spine maintenance / cupric ion binding / cell surface receptor signaling pathway via STAT / regulation of potassium ion transmembrane transport / enterobactin binding / positive regulation of insulin-like growth factor receptor signaling pathway / Heme biosynthesis / HDL remodeling / IgG binding / negative regulation of mitochondrial depolarization / negative regulation of calcineurin-NFAT signaling cascade / growth hormone receptor signaling pathway / Prednisone ADME / Heme degradation / positive regulation of peptidyl-tyrosine phosphorylation / negative regulation of interleukin-2 production / negative regulation of T cell receptor signaling pathway / Aspirin ADME / Prolactin receptor signaling / negative regulation of activated T cell proliferation / negative regulation of amyloid-beta formation / beta-2-microglobulin binding / cuprous ion binding / antioxidant activity / negative regulation of type II interferon production / negative regulation of protein phosphorylation / growth hormone receptor signaling pathway via JAK-STAT / positive regulation of protein targeting to membrane / Synthesis, secretion, and deacylation of Ghrelin / cell surface receptor signaling pathway via JAK-STAT / toxic substance binding / Scavenging of heme from plasma / Growth hormone receptor signaling / Recycling of bile acids and salts / side of membrane / inclusion body / cellular response to copper ion / neuron projection maintenance / positive regulation of MAP kinase activity / platelet alpha granule lumen / molecular function activator activity / cellular response to starvation / fatty acid binding / cytokine activity / endosome lumen / positive regulation of receptor signaling pathway via JAK-STAT / positive regulation of protein localization to plasma membrane / Post-translational protein phosphorylation / growth factor activity / molecular condensate scaffold activity / response to nutrient levels / cytokine-mediated signaling pathway / protein destabilization / terminal bouton / Cytoprotection by HMOX1 / hormone activity / protein homooligomerization / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / cellular response to amyloid-beta / pyridoxal phosphate binding / positive regulation of neuron apoptotic process / Platelet degranulation / cellular response to xenobiotic stimulus / response to estradiol / signaling receptor activity / amyloid-beta binding / protein-folding chaperone binding / protease binding / microtubule binding / nuclear membrane / blood microparticle / response to oxidative stress / learning or memory / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endosome membrane / immune response / membrane raft / copper ion binding / endoplasmic reticulum lumen / external side of plasma membrane / dendrite / protein-containing complex binding

Domain/homology:

Somatotropin / Somatotropin/prolactin / Somatotropin hormone, conserved site / Somatotropin hormone family / Somatotropin, prolactin and related hormones signature 1. / Somatotropin, prolactin and related hormones signature 2. / Major prion protein N-terminal domain / Major prion protein bPrPp - N terminal / Prion protein signature 1. / Prion protein signature 2. / Prion protein / Major prion protein / Prion/Doppel protein, beta-ribbon domain / Prion/Doppel beta-ribbon domain superfamily / Prion/Doppel alpha-helical domain / Serum albumin/Alpha-fetoprotein/Afamin / ALB/AFP/VDB / Serum albumin, N-terminal / Serum albumin, conserved site / Serum albumin-like / Serum albumin family / Albumin domain signature. / Albumin domain profile. / serum albumin / Four-helical cytokine-like, core / Class I Histocompatibility antigen, domains alpha 1 and 2 / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold

Component:

Somatotropin / Albumin / IgG receptor FcRn large subunit p51 / Major prion protein

• Biological species: Homo sapiens (human)

Contact author

• Eva Johansson (Novo Nordisk A/S)

Models

Sample

• Sample: Name: Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the human growth hormone derivative somapacitan.; Specimen concentration: 4.5 mg/ml / Entity id: 1462 / 1464 / 1467 / 1475
• Buffer: Name: 100 mM MES, 100 mM NaCl / pH: 6.5

Entity #1462

Type: protein / Description: somapacitan / Formula weight: 22.119 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P01241
Sequence:

FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS CVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F

Entity #1464

Name: HSAopt / Type: protein
Description: FcRn binding optimised human serum albumin V418M, T420A, E505G, V547A
Formula weight: 66.373 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P02768
Sequence:

DAHKSEVAHR FKDLGEENFK ALVLIAFAQY LQQCPFEDHV KLVNEVTEFA KTCVADESAE NCDKSLHTLF GDKLCTVATL RETYGEMADC CAKQEPERNE CFLQHKDDNP NLPRLVRPEV DVMCTAFHDN EETFLKKYLY EIARRHPYFY APELLFFAKR YKAAFTECCQ AADKAACLLP KLDELRDEGK ASSAKQRLKC ASLQKFGERA FKAWAVARLS QRFPKAEFAE VSKLVTDLTK VHTECCHGDL LECADDRADL AKYICENQDS ISSKLKECCE KPLLEKSHCI AEVENDEMPA DLPSLAADFV ESKDVCKNYA EAKDVFLGMF LYEYARRHPD YSVVLLLRLA KTYETTLEKC CAAADPHECY AKVFDEFKPL VEEPQNLIKQ NCELFEQLGE YKFQNALLVR YTKKVPQMSA PTLVEVSRNL GKVGSKCCKH PEAKRMPCAE DYLSVVLNQL CVLHEKTPVS DRVTKCCTES LVNRRPCFSA LEVDETYVPK EFNAGTFTFH ADICTLSEKE RQIKKQTALV ELVKHKPKAT KEQLKAAMDD FAAFVEKCCK ADDKETCFAE EGKKLVAASQ AALGL

Entity #1467

Name: FcRn ECD beta / Type: protein
Description: neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag
Formula weight: 12.554 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P61768
Sequence:

IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC RVNHVTLSQP KIVKWDRDMH HHHHH

Entity #1475

Name: FcRn ECD alpha / Type: protein / Description: neonatal Fc receptor ectodomain alpha-chain / Formula weight: 30.375 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P55899
Sequence:

AESHLSLLYH LTAVSSPAPG TPAFWVSGWL GPQQYLSYNS LRGEAEPCGA WVWENQVSWY WEKETTDLRI KEKLFLEAFK ALGGKGPYTL QGLLGCELGP DNTSVPTAKF ALNGEEFMNF DLKQGTWGGD WPEALAISQR WQQQDKAANK ELTFLLFSCP HRLREHLERG RGNLEWKEPP SMRLKARPSS PGFSVLTCSA FSFYPPELQL RFLRNGLAAG TGQGDFGPNS DGSFHASSSL TVKSGDEHHY CCIVQHAGLA QPLRVELESP AKSS

Experimental information

• Beam: Instrument name: MAX IV I911-4 / City: Lund / 国: Sweden / Type of source: X-ray synchrotron / Wavelength: 0.1 Å
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the human growth hormone derivative somapacitan.
Measurement date: May 11, 2015 / Storage temperature: 25 °C / Cell temperature: 25 °C / Exposure time: 120 sec. / Number of frames: 1 / Unit: 1/A /

	Min	Max
Q	0.0094	0.4379

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 306 /

	Min	Max
Q	0.01062	0.1906
P(R) point	3	308
R	0	146.6

Result

Type of curve: single_conc /

	Experimental	Porod
MW	130 kDa	132 kDa
Volume	-	227 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	0.4737	0.4742	0.001
Radius of gyration, Rg	4.2 nm	4.15 nm	0.01

	Min	Max
D	-	14.66
Guinier point	3	38