Structural highlights
Function
[ZN174_HUMAN] Transcriptional repressor.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Retroviral assembly is driven by multiple interactions mediated by the Gag polyprotein, the main structural component of the forming viral shell. Critical determinants of Gag oligomerization are contained within the C-terminal domain (CTD) of the capsid protein, which also harbors a conserved sequence motif, the major homology region (MHR), in the otherwise highly variable Gag. An unexpected clue about the MHR function in retroviral assembly emerges from the structure of the zinc finger-associated SCAN domain we describe here. The SCAN dimer adopts a fold almost identical to that of the retroviral capsid CTD but uses an entirely different dimerization interface caused by swapping the MHR-like element between the monomers. Mutations in retroviral capsid proteins and functional data suggest that a SCAN-like MHR-swapped CTD dimer forms during immature particle assembly. In the SCAN-like dimer, the MHR contributes the major part of the large intertwined dimer interface explaining its functional significance.
Mammalian SCAN domain dimer is a domain-swapped homolog of the HIV capsid C-terminal domain.,Ivanov D, Stone JR, Maki JL, Collins T, Wagner G Mol Cell. 2005 Jan 7;17(1):137-43. PMID:15629724[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Williams AJ, Khachigian LM, Shows T, Collins T. Isolation and characterization of a novel zinc-finger protein with transcription repressor activity. J Biol Chem. 1995 Sep 22;270(38):22143-52. PMID:7673192
- ↑ Ivanov D, Stone JR, Maki JL, Collins T, Wagner G. Mammalian SCAN domain dimer is a domain-swapped homolog of the HIV capsid C-terminal domain. Mol Cell. 2005 Jan 7;17(1):137-43. PMID:15629724 doi:10.1016/j.molcel.2004.12.015