5I50,5I50,5I4Z,5I4Z,6G6J,6G6J,6G6K,6G6K,6G6L,6G6L,6G6L,6G6L,8OTS,1NKP,1NKP


Conserved Protein Domain Family
Myc-LZ
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pfam02344: Myc-LZ (This model is not part of the current CDD release)
Myc leucine zipper domain
This family consists of the leucine zipper dimerization domain found in both cellular c-Myc proto-oncogenes and viral v-Myc oncogenes. dimerization via the leucine zipper motif with other basic helix-loop-helix-leucine zipper (b/HLH/lz) proteins such as Max is required for efficient DNA binding. The Myc-Max dimer is a transactivating complex activating expression of growth related genes promoting cell proliferation. The dimerization is facilitated via interdigitating leucine residues every 7th position of the alpha helix. Like charge repulsion of adjacent residues in this region perturbs the formation of homodimers with heterodimers being promoted by opposing charge attractions.
Links
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Statistics
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PSSM-Id: 514874
Aligned: 144 rows
Threshold Bit Score: 30.7111
Created: 13-Feb-2025
Updated: 28-Apr-2025
Structure
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Program:
Drawing:
Aligned Rows:
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PubMed ReferencesClick to see Conserved Features Help
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
5I50_A         87 AETQKLISEIDLLRKQNEQLKHKLEQLRNsC 117 human
NP_001265781  342 GDERKLLTTKEELRKRSRELKRRLEQLRTlH 372
XP_026169546  364 EDERRLLKMKDELRKRSRELKHRLERLRTsH 394
20_pfamImport   1 EDERRLLTMKDELRKRSRELKHTLQQLRTlH 31 
XP_022074371  336 EDESRLLTAKDELRKRSRELKHRLQQLRTlR 366
P52160        389 LDEQRLLSIKEQLRRKSEQLKHRLQQLRSsH 419 zebrafish
XP_013994567  369 MDEQKLLLLKEQLRKKSEQLTSRLEQLRNsQ 399
XP_010891384  375 SDEQKLLSLKEQLRGKREKLKQRLEQLRNsQ 405
XP_007258657  363 SDEQKLLSIKEQLRRKSEQLKHRLQLLRRsQ 393
P49709        369 lDEQRLLSIKEQLRRKSEQLKHRLQQLRSsH 399 goldfish
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