1E0O,1EV2,1CVS,1RY7


Conserved Protein Domain Family
Ig2_FGFR

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cd05857: Ig2_FGFR 
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Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor
Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.
Statistics
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PSSM-Id: 143265
View PSSM: cd05857
Aligned: 8 rows
Threshold Bit Score: 170.426
Threshold Setting Gi: 114149298
Created: 11-Jan-2008
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
FGF bindingligand binding
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:FGF binding site [polypeptide binding site]
Evidence:
  • Structure:1E0O_B; human FGF1-FGFR2 interaction interface defined by 3.5A distance.
    View structure with Cn3D
  • Comment:The FGF1-FGFR2-heparin complex is comprised of one heparin molecule linked to two FGF1 molecules, each FGF1 molecule of which is bound to a receptor ectodomain. Shown here is one FGF1 molecule bound to the receptor ectodomain.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          # # #                                                                         
1E0O_B        17 KRLHAVPAANTVKFRCPAGgnPMPTMRWLKNGkEFKQEHRIGGYKVRNqHWSLIMESVVPSDKGNYTCVVENeYGSINHT 96
1EV2_E        18 KRLHAVPAANTVKFRCPAGgnPMPTMRWLKNGkEFKQEHRIGGYKVRNqHWSLIMESVVPSDKGNYTCVVENeYGSINHT 97
1CVS_C        23 KKLHAVPAAKTVKFKCPSSgtPQPTLRWLKNGkEFKPDHRIGGYKVRYaTWSIIMDSVVPSDKGNYTCIVENeYGSINHT 102
1RY7_B       130 KKLLAVPAANTVRFRCPAAgnPTPSISWLKNGrEFRGEHRIGGIKLRHqQWSLVMESVVPSDRGNYTCVVENkFGSIRQT 209
gi 114149298  84 KRLHAEPAGNTVQFRCAVQgaRPITVDWYKDGePIKKNGRLGGYKFRQrNQQISLESVIMSDRAKYMCVAHNkYGSINHT 163
gi 45384352  166 KRLHAVPAANTVKFRCPAMgnPTPTMRWLKNGkEFKQEHRIGGYKVRNqHWSLIMESVVPSDKGNYTCIVENqYGSINHT 245
gi 544293    155 KKLHAVSAANTVKLRCPARe-PHPSNEWLKNGkEFKQEHRIGGYKVRNqHWSLIMESVVPSDKGIYTCIVENeHGSINHT 233
gi 82102599  164 KKLHAVPAANTVKFRCAAAgnPKPKMRWLKNAkPFRQEDRMGGYKVRLqHWTLIMESVVPSDKGNYTCLVENqYGSIDHT 243

                 ....*
Feature 1             
1E0O_B        97 YHLDV 101
1EV2_E        98 YHLDV 102
1CVS_C       103 YQLDV 107
1RY7_B       210 YTLDV 214
gi 114149298 164 YELDV 168
gi 45384352  246 YHLDV 250
gi 544293    234 YHLDV 238
gi 82102599  244 YTLDV 248

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