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- EMDB-71047: Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinemen... -

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Basic information

Entry
Database: EMDB / ID: EMD-71047
TitleCryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1.
Map dataCryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1.
Sample
  • Complex: Chicken ROS1 receptor
    • Protein or peptide: Tyrosine-protein kinase receptor
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
KeywordsROS1 / STRUCTURAL PROTEIN
Function / homology
Function and homology information


columnar/cuboidal epithelial cell development / regulation of phosphate transport / regulation of TOR signaling / regulation of ERK1 and ERK2 cascade / transmembrane receptor protein tyrosine kinase activity / cell surface receptor protein tyrosine kinase signaling pathway / receptor protein-tyrosine kinase / protein phosphatase binding / spermatogenesis / gene expression ...columnar/cuboidal epithelial cell development / regulation of phosphate transport / regulation of TOR signaling / regulation of ERK1 and ERK2 cascade / transmembrane receptor protein tyrosine kinase activity / cell surface receptor protein tyrosine kinase signaling pathway / receptor protein-tyrosine kinase / protein phosphatase binding / spermatogenesis / gene expression / signaling receptor complex / negative regulation of gene expression / perinuclear region of cytoplasm / cell surface / ATP binding / plasma membrane
Similarity search - Function
LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Six-bladed beta-propeller, TolB-like / Fibronectin type III domain / : / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III ...LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Six-bladed beta-propeller, TolB-like / Fibronectin type III domain / : / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Tyrosine-protein kinase receptor
Similarity search - Component
Biological speciesGallus gallus (chicken)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsBai XC / Zhang XW
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Nat Commun / Year: 2026
Title: Structural insights into the activation of the chicken ROS1 receptor by the NEL/NICOL ligand complex.
Authors: Weidong An / Xuewu Zhang / Xiao-Chen Bai /
Abstract: The receptor tyrosine kinase ROS1 plays essential roles in cell growth and sperm maturation, yet its activation mechanism has remained poorly understood. Here, we report high-resolution cryo-electron ...The receptor tyrosine kinase ROS1 plays essential roles in cell growth and sperm maturation, yet its activation mechanism has remained poorly understood. Here, we report high-resolution cryo-electron microscopy (cryo-EM) structures of chicken ROS1 in its ligand-free form, in complex with its ligand NEL, and with the ligand/co-ligand complex NEL/NICOL. Unliganded ROS1 adopts an arc-shaped conformation. The interaction between NEL and ROS1 is mediated by the VWC2 domain of NEL and the β1 domain of ROS1. Binding of NICOL to the coiled-coil domain of NEL stabilizes NEL into a batwing-shaped asymmetric dimer, which can recruit only one ROS1 molecule due to steric hindrance. Structural analyses and biochemical results suggest that the 2:1 NEL/NICOL complexes further oligomerize through LamG-VWC4 domain interactions, facilitating the clustering of multiple ROS1 for its activation. Functional assays confirm that both NICOL and the multimerization of NEL/NICOL complexes are required for robust ROS1 signaling. Our findings establish NICOL as a critical co-ligand for ROS1 and suggest a distinct ligand-driven oligomerization mechanism for ROS1 activation.
History
DepositionJun 4, 2025-
Header (metadata) releaseFeb 25, 2026-
Map releaseFeb 25, 2026-
UpdateApr 8, 2026-
Current statusApr 8, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_71047.png

Downloads & links

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Map

FileDownload / File: emd_71047.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.18 Å/pix.
x 350 pix.
= 413. Å		1.18 Å/pix.
x 350 pix.
= 413. Å		1.18 Å/pix.
x 350 pix.
= 413. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.18 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.0318514 - 0.07078724
Average (Standard dev.)0.000050093284 (±0.0007885618)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 412.99997 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM...

Fileemd_71047_half_map_1.map
AnnotationCryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1, half map1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM...

Fileemd_71047_half_map_2.map
AnnotationCryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1, half map2.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Chicken ROS1 receptor

EntireName: Chicken ROS1 receptor
Components
  • Complex: Chicken ROS1 receptor
    • Protein or peptide: Tyrosine-protein kinase receptor
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Chicken ROS1 receptor

SupramoleculeName: Chicken ROS1 receptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Gallus gallus (chicken)

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Macromolecule #1: Tyrosine-protein kinase receptor

MacromoleculeName: Tyrosine-protein kinase receptor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: receptor protein-tyrosine kinase
Source (natural)Organism: Gallus gallus (chicken)
Molecular weightTheoretical: 261.174797 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRNACLLLNR LGAFYFIWIS AAYCSFSKNC QDLCTSNLEG ELGIANLCNV SDINVACTQG CQFWNATEQV NCPLKCNKTY TRECETVSC KFGCSRAEDA YGVEAQNCLN KPGAPFASSI GSHNITLGWK PANISEVKYI IQWKFHQLPG DWRYTEVVSE T SYTVKDLQ ...String:
MRNACLLLNR LGAFYFIWIS AAYCSFSKNC QDLCTSNLEG ELGIANLCNV SDINVACTQG CQFWNATEQV NCPLKCNKTY TRECETVSC KFGCSRAEDA YGVEAQNCLN KPGAPFASSI GSHNITLGWK PANISEVKYI IQWKFHQLPG DWRYTEVVSE T SYTVKDLQ AFTEYEFRVV WIITSQLQLH SPPSPSYRTH ASGVPTTAPI IKDIQSSSPN TVEVSWFPPL FPNGLIVGYN LV LTSENHE LLRASRGHSF QFYSTFPNST YRFSIVAVNE AGAGPPAEAN ITTPESKVKE KAKWLFLSRN QSLRKRYMEH FLE AAHCLQ NGIIHHNITG ISVNVYQQVV YFSEGNSIWV KGVVDMSDVS DLTLFYTGWG NITSISVDWL YQRMYFVMNE KIHV CQLEN CTAAEDITPP YVTSPRKIVA DPYNGYIFCL LEDGIYRANL PLFPDTASAA SLVVKSHTLR DFMINFQSKR LIFFN KTEQ AFVSGFLDGS EFHTLRAHVP LDDMESFVYE DNIFTVTDGR AVFHEEISQV GSSSFNEYVV DCSLEYPEYF GFGNLL FYA ASTQPYPLPT LPRLVTVLFG SDQAVISWSP PEYTIGTSRS AWQNWTYDVK VSSQSTFEEE WVVSNITDTR FAVKNLV SF TEYEMSVRAV SPAGEGPWSE PFRGMTFEEA EEEPYILAVG AEGLWKQRLD SYGPGEFLYP HIRNISDLDW YNDTLYWS N SMGKVQTWSM NKKEGTTENS YVPDIKNARM LAFDWLGQCL YWAGKANTIY RKSLLGDHMD VVAHVVYVVK DLAVDSVNG YLYWATTYTV ESARLNGEEY LILQEHLQFS GKQVVGLALD LTSGFLYWLV QDGLCLNLYR ISICKESCGN IMVTEISAWS VSEVSQNAL QYYSGRLFWI NRLKFITTQE LNQSISIPFS EPAEFAAFTL VHTSLKPLPG NFSFTPKVIP SSVPESSFKI K GNSSSFHI IWNASTDVQW GTVFYCVGSN ALQMRTLESE RCLHPHDLTV PSYKVDWLEP FTLFDFSVTP YTYWGKAPTT SV YLRAPEG VPSAPANPRI YVLHSNTHEG EEKVLVELRW DKPERDNGVL TQFRVYYQLL YESGAADTLM EWNVSDVKPT ALL FSIRDV HPRLTVRFQV QAFTSVGPGP MSDVAQRNSS DIFPVPTLIT FSSNKLFLTD IDSNHTIWEV LTNRNIKDIC YTAD DDKVY YILEDSLFLL NVQSTSESQL FEDVFLRNVT AITVDWIARH LFVAMKTSWN ETQVFFIDLE LKTKSLKALN IQLGK RNST ISSLLSYPFL SRLYWIEELD YGSRMFYYDI LNNTMYHILG YESVEEKMRN YCNCNVAEAE LGRPISIDVT DIKKPQ LLF IRGRDEIWAS DVDGCHCWRI TKIPSFQGTK IGSLTVDKQF IYWTIEKKEY TEICLADKES TRHSLQRKAN HELKILA YS SAMQSYPDKK CLTPLLDTEK PTILDTTNTS FTLSLPSVTT QQLCPSISQP TPTYLVFFRE ITSNHENSTY HFSTLLQK T LEIQEPIAVI NNLKPFSSYA IQVAVKNYYS NQNQLAVGRE TISTTLYGVP EGVDSIKTVV LSDTTINISW SEPLEPNGP LESIRYQISV NLLSLFPEAP LRKSEFPNGT LSWSVSDLQS GTNNLFKVLA FHPNENWFSE SVPVIAKTFE TPLSPSNIIP RNTSFQLEW RAPLHINGTS FWFELRKWQT RSDWFSPAST TCTVGPVYTC NLTGTLPSAN YLVRATVVYV TGMKSTSSPT S FKTTAGVP SKPGTPKRAE DSKNSVQWEK AEDNGSNLTY YILESRKQSG NTNKVKSLWV VVYNGSCDSI CTWKAENLEG TF QFRAAAA NMLGLGEYSD TSKDIVLAKD TVTSPDITAI VAVIGAVVLG LTIIILFGFV WHQRWKSRKP ASTGQIVLVK EDK ELAQLR GMAETVGLAN ACYAVSTLPS QAEIESLPAF PRDKLNLHKL LGSGAFGEVY EGTALDILAD GSGESRVAVK TLKR GATDQ EKSEFLKEAH LMSKFDHPHI LKLLGVCLLN EPQYLILELM EGGDLLSYLR GARKQKFQSP LLTLTDLLDI CLDIC KGCV YLEKMRFIHR DLAARNCLVS EKQYGSCSRV VKIGDFGLAR DIYKNDYYRK RGEGLLPVRW MAPESLIDGV FTNHSD VWA FGVLVWETLT LGQQPYPGLS NIEVLHHVRS GGRLESPNNC PDDIRDLMTR CWAQDPHNRP TFFYIQHKLQ EIRHSPL CF SYFLGDKESV AGFINQAFED IDVPPADSDS ILSTTLMEAR DQEGLNYLVV VKESNQDQGS ISSAELTSV

UniProtKB: Tyrosine-protein kinase receptor

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Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 10 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration8 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: Gctf / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: Made by RELION
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 255602
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final 3D classificationSoftware - Name: RELION

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Atomic model buiding 1

RefinementProtocol: AB INITIO MODEL
Output model

PDB-9oz1:
Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1.

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