2Q0N,2CDZ,2X4Z


Conserved Protein Domain Family
STKc_PAK4

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cd06657: STKc_PAK4 
Click on image for an interactive view with Cn3D
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4
STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Statistics
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PSSM-Id: 132988
View PSSM: cd06657
Aligned: 6 rows
Threshold Bit Score: 574.663
Threshold Setting Gi: 151567918
Created: 16-Nov-2007
Updated: 2-Mar-2014
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 22 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:
  • Structure:2CDZ; Human PAK4 binds the purine-based inhibitor Cgp74514a; defined at 4A contacts.
    View structure with Cn3D
  • Structure:2X4Z; Human PAK4 binds inhibitor Pf-03758309; contacts at 4A.
    View structure with Cn3D
  • Comment:Also based on the structure of PAK5 bound to purine-based inhibitor that mimics the binding of ATP, and on the binding of other related proteins with structure to ATP or inhibitors.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                   #####   #            # #                            #
2Q0N_A        10 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 89
2CDZ_A        12 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 91
2X4Z_A         5 SHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 84
gi 14330664  359 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATIKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 438
gi 50345106  372 SHEQFRAALQMVVDPGDPRTYLDHYIKIGEGSTGIVCIATVKTTGKLVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVV 451
gi 363746159 267 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                       ##### ##  #                                      ## #         ## 
2Q0N_A        90 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 169
2CDZ_A        92 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 171
2X4Z_A        85 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 164
gi 14330664  439 EMYNSYLVGDELWVIMEFLEGGALTDIVTHTRMNEEQIATVCVSVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 518
gi 50345106  452 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQISTVCLSVLKALSVLHSQGVIHRDIKSDSILLTHDGRVKLSDF 531
gi 363746159 347 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
2Q0N_A       170 GFCAQVSKEVPRRKXLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 249
2CDZ_A       172 GFCAQVSKEVPRRKXLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 251
2X4Z_A       165 GFCAQVSKEVPRRKXLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLH 244
gi 14330664  519 GFCAQVNKEVPRRKSLVGTPYWMAPELISRLPYGPEVDVWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNAQ 598
gi 50345106  532 GFCAQVSKEVQRRKSLVGTPYWMAPELISRLPYGPEVDIWSFGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 611
gi 363746159 427 GFCAQVNKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGVMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNVH 506
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
Feature 1                                                            
2Q0N_A       250 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 301
2CDZ_A       252 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 303
2X4Z_A       245 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR 296
gi 14330664  599 KVSPLLKGFLDRLLVRDPSQRASANELLKHPFLGKAGPPSCIVPLMRQNRMR 650
gi 50345106  612 KVSPLLKGFLDRMLVRDPAQRATAQELLKHPFLTKAGPPSCIVPLMRQNRMR 663
gi 363746159 507 KVSPSLKGFLDRMLVRDPVQRATANELLKHPFLGKAGPPSCIVPLMRQNRMR 558

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