1t94
From Proteopedia
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Crystal structure of the catalytic core of human DNA polymerase kappa
Overview
We present the crystal structure of the catalytic core of human DNA polymerase kappa (hPolkappa), the first structure of a human Y-family polymerase. hPolkappa is implicated in the proficient extension of mispaired primer termini on undamaged DNAs, and in the extension step of lesion bypass. The structure reveals a stubby "fingers" subdomain, which despite its small size appears to be tightly restrained with respect to a putative templating base. The structure also reveals a novel "thumb" subdomain that provides a basis for the importance of the N-terminal extension unique to hPolkappa. And, most surprisingly, the structure reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal side of the "palm" subdomain, as opposed to the fingers subdomain. Together, these properties suggest that the hPolkappa active site is constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the lesion.
About this Structure
1T94 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic core of human DNA polymerase kappa., Uljon SN, Johnson RE, Edwards TA, Prakash S, Prakash L, Aggarwal AK, Structure. 2004 Aug;12(8):1395-404. PMID:15296733
Page seeded by OCA on Thu Feb 21 15:11:13 2008
