Tumor necrosis factor ligand superfamily member 11

UniProt data

UniProt name: TNF11_HUMAN (O14788)

Gene name: TNFSF11; Synonyms=OPGL, RANKL, TRANCE

Organism: Homo sapiens (Human).

Function: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (PubMed:22664871). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (By similarity). {ECO:0000250|UniProtKB:O35235, ECO:0000269|PubMed:22664871}.

Subcellular location: Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted {ECO:0000250}.

Transmembrane domains:

  1. 48-68, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.

Sequence: 317 AA

10 20 30 40 50 60 MRRASRDYTK YLRGSEEMGG GPGAPHEGPL HAPPPPAPHQ PPAASRSMFV ALLGLGLGQV 70 80 90 100 110 120 VCSVALFFYF RAQMDPNRIS EDGTHCIYRI LRLHENADFQ DTTLESQDTK LIPDSCRRIK 130 140 150 160 170 180 QAFQGAVQKE LQHIVGSQHI RAEKAMVDGS WLDLAKRSKL EAQPFAHLTI NATDIPSGSH 190 200 210 220 230 240 KVSLSSWYHD RGWAKISNMT FSNGKLIVNQ DGFYYLYANI CFRHHETSGD LATEYLQLMV 250 260 270 280 290 300 YVTKTSIKIP SSHTLMKGGS TKYWSGNSEF HFYSINVGGF FKLRSGEEIS IEVSNPSLLD 310 PDQDATYFGA FKVRDID

CATM prediction

The sequence of TNF11_HUMAN returned 3 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
       50        60        70
+    |    +    |    +    | 		 (Å) (°) (Å) (°)  
Model 1 SRSMFVALLGLGLGQVVCSVALFFYFR 6.5 -42.8° 6.0 44.0 -36.7
Model 2 SRSMFVALLGLGLGQVVCSVALFFYFR 6.9 -53.0° 1.9 45.0 -18.1
Model 3 SRSMFVALLGLGLGQVVCSVALFFYFR 7.4 -50.0° 2.9 46.9 -6.7

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 51, ALA, HA A, 50, VAL, O 3.26Å
B, 54, GLY, HA1 A, 51, ALA, O 2.70Å
B, 55, LEU, HA A, 54, GLY, O 2.43Å
B, 58, GLY, HA1 A, 55, LEU, O 3.10Å
A, 51, ALA, HA B, 50, VAL, O 3.26Å
A, 54, GLY, HA1 B, 51, ALA, O 2.70Å
A, 55, LEU, HA B, 54, GLY, O 2.43Å
A, 58, GLY, HA1 B, 55, LEU, O 3.10Å