1ik9
From Proteopedia
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CRYSTAL STRUCTURE OF A XRCC4-DNA LIGASE IV COMPLEX
Contents |
Overview
A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental, role in DNA non-homologous end joining (NHEJ), a cellular function, required for double-strand break repair and V(D)J recombination. Here we, report the crystal structure of human Xrcc4 bound to a polypeptide that, corresponds to the DNA ligase IV sequence linking its two BRCA1 C-terminal, (BRCT) domains. In the complex, a single ligase chain binds asymmetrically, to an Xrcc4 dimer. The helical tails of Xrcc4 undergo a substantial, conformational change relative to the uncomplexed protein, forming a, coiled coil that unwinds upon ligase binding, leading to a flat, interaction surface. A buried network of charged hydrogen bonds surrounded, by extensive hydrophobic contacts explains the observed tightness of the, interaction. The strong conservation of residues at the interface between, the two proteins provides evidence that the observed mode of interaction, has been maintained in NHEJ throughout evolution.
Disease
Known diseases associated with this structure: LIG4 syndrome OMIM:[601837], Multiple myeloma, resistance to OMIM:[601837]
About this Structure
1IK9 is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1IK9 with [DNA Ligase]. Active as DNA ligase (ATP), with EC number 6.5.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of an Xrcc4-DNA ligase IV complex., Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L, Nat Struct Biol. 2001 Dec;8(12):1015-9. PMID:11702069
Page seeded by OCA on Fri Feb 15 16:01:57 2008
