1a3q
From Proteopedia
HUMAN NF-KAPPA-B P52 BOUND TO DNA
Overview
The crystal structure of human NF-kappaB p52 in its specific complex with the natural kappaB DNA binding site MHC H-2 has been solved at 2.1 A resolution. Whereas the overall structure resembles that of the NF-kappaB p50-DNA complex, pronounced differences are observed within the 'insert region'. This sequence segment differs in length between different Rel proteins. Compared with NF-kappaB p50, the compact alpha-helical insert region element is rotated away from the core of the N-terminal domain, opening up a mainly polar cleft. The insert region presents potential interaction surfaces to other proteins. The high resolution of the structure reveals many water molecules which mediate interactions in the protein-DNA interface. Additional complexity in Rel protein-DNA interaction comes from an extended interfacial water cavity that connects residues at the edge of the dimer interface to the central DNA bases. The observed water network might acount for differences in binding specificity between NF-kappaB p52 and NF-kappaB p50 homodimers.
About this Structure
1A3Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1 A resolution., Cramer P, Larson CJ, Verdine GL, Muller CW, EMBO J. 1997 Dec 1;16(23):7078-90. PMID:9384586 Page seeded by OCA on Fri May 2 09:46:02 2008
