Conserved Protein Domain Family
PB1_Mekk2_3

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cd06405: PB1_Mekk2_3 
Click on image for an interactive view with Cn3D
The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain.
Statistics
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PSSM-Id: 99726
View PSSM: cd06405
Aligned: 7 rows
Threshold Bit Score: 127.503
Threshold Setting Gi: 158600074
Created: 27-Feb-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
PB1 interaction
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:PB1 interaction [polypeptide binding site]
Evidence:
  • Structure:2O2V; Human MAP2K5 and MAP3K3 form an asymmetric heterodimer
    View structure with Cn3D
  • Comment:MEK2/3 contains a type II PB1 domain and Map2K5 contains a type I PB1 domain

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1         # #     ###               #                                               #  # 
2NPT_B        21 VRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQsMDLHYTNNe----lVIPLTTQDDLDKAVELldr--sihMKSLKI 94
2O2V_B        11 VRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQpLDLHYMNNe----lSILLKNQDDLDKAIDIldr--sssMKSLRI 84
gi 115943014  42 IRVKFEFNGEKRILQIPRPLKYDDILLKARTTFGQpVDMFLTNHnttfslLIPIRDQTDLNHAVEItdn--npnAKSLRL 119
gi 119331086  42 VRIKFEYEGEKRIIQFPRPVKFKEVVQKVTDAFGQtMDLVCMSNe----lLIPLKSQEDLDKAMEQlel--spsLKSLRI 115
gi 147902148  36 ARIKFEYNGEKRIIEFRRPIKLKDVQQKVTDAFGQtMDLHYTNDe----lLIPLVCQEDMDRALEYlda--cpaLKSLRI 109
gi 157787113  57 LRVKLEHEREKRIIPFQRPLKFKDLLQKVTEAFGQqMDLYFTEKe----mLVALKCQEDLDRAIQGlsss-sgmNNLLRV 131
gi 158600074  55 IRIKAEFRGEKFCFEMHRPVIFDELQMHLNSRCNFkLNIYYTLRnh--elIVPIRNQLELDRAIELvdfdrtshQRSLRL 132

                 ....*
Feature 1             
2NPT_B        95 LLVIN 99
2O2V_B        85 LLLSQ 89
gi 115943014 120 HLELA 124
gi 119331086 116 LVSAP 120
gi 147902148 110 LVKAP 114
gi 157787113 132 ILKTP 136
gi 158600074 133 LLSRY 137

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