1EV2


Conserved Protein Domain Family
Ig3_FGFR-2

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cd05858: Ig3_FGFR-2 
Click on image for an interactive view with Cn3D
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2)
Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.
Statistics
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PSSM-Id: 143266
View PSSM: cd05858
Aligned: 5 rows
Threshold Bit Score: 150.084
Threshold Setting Gi: 114149298
Created: 11-Jan-2008
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
polypeptide
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:polypeptide ligand binding site [polypeptide binding site]
Evidence:
  • Structure:1EV2_A; Fiboblast Growth Factor 2 (FGF2) complexed with the Ig-like domains D2 and D3 of FGF receptor 2 (FGFR2), contacts based on 3.5 A distance.
    View structure with Cn3D
  • Comment:The Ig-like domains D2 and D3 and the loop that connects them define the general binding site.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                  #    ###                            ##   #   #                    #   
1EV2_E       125 GGDVEFVCK-VYSDAQPHIQWIKHvekngskygpdglPYLKVLKaaGVNTTDKEIEVLYIrnvtfedAGEYTCLAGNSIG 203
gi 116097    262 GSNVEFHCK-VYSDAQPHIQWLKHvevngskygpdgtPYVTVLKtaGVNTTDKELEILYLrnvtfedAGEYTCLAGNSIG 340
gi 82102599  271 GQDAKFVCK-VYSDAQPHIQWLQHytkngsccgpdglPYVRVLKtaGVNTTDKEIEVLYLpnvtfedAGEYTCLAGNSIG 349
gi 120048    266 GTTAEFSCK-VYSDPQPHIQWLRHieingsrvasdgfPYVEILKtaGVNTSDKDMEVLHLrnvtfedAGQYTCLAANSIG 344
gi 114149298 191 GSTVTFRCRiVYSDAHPHVEWLKYn------------VNVTVLKraGINTTDAEMEKLTLknvsfadAGEYTCLAGNSIG 258
                         90
                 ....*....|.
Feature 1                   
1EV2_E       204 ISFHSAWLTVL 214
gi 116097    341 FSHHSAWLTVL 351
gi 82102599  350 ISYHTAWLTVH 360
gi 120048    345 ISHHSAWLTVL 355
gi 114149298 259 VSHVSAWLTVL 269

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