Member database | Pfam |
Pfam type | domain |
Short name | zf-DNA_Pol |
Author | Mistry J;0000-0003-2479-5322 Sammut SJ;0000-0003-4472-904X |
Sequence Ontology | 0000417 |
Description
The DNA Polymerase alpha zinc finger domain adopts an alpha-helix-like structure, followed by three turns, all of which involve proline. The resulting motif is a helix-turn-helix motif, in contrast to other zinc finger domains, which show anti-parallel sheet and helix conformation. Zinc binding occurs due to the presence of four cysteine residues positioned to bind the metal centre in a tetrahedral coordination geometry. Function of this domain is uncertain: it has been proposed that the zinc finger motif may be an essential part of the DNA binding domain
[1].
References
1.Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha. Evanics F, Maurmann L, Yang WW, Bose RN. Biochim. Biophys. Acta 1651, 163-71, (2003). View articlePMID: 14499601