1y7q
From Proteopedia
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Mammalian SCAN domain dimer is a domain-swapped homologue of the HIV capsid C-terminal domain
Overview
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.
About this Structure
1Y7Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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