1dml

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[[Image:1dml.gif|left|200px]]
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{{STRUCTURE_1dml| PDB=1dml | SCENE= }}
{{STRUCTURE_1dml| PDB=1dml | SCENE= }}
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'''CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL'''
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===CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL===
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==Overview==
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Herpes simplex virus DNA polymerase is a heterodimer composed of a catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal structure of a complex of the C-terminal 36 residues of Pol bound to residues 1-319 of UL42 reveals remarkable similarities between UL42 and PCNA despite contrasting biochemical properties and lack of sequence homology. Moreover, the Pol-UL42 interaction resembles the interaction between the cell cycle regulator p21 and PCNA. The structure and previous data suggest that the UL42 monomer interacts with DNA quite differently than does multimeric toroidal PCNA. The details of the structure lead to a model for the mechanism of UL42, provide the basis for drug design, and allow modeling of other proteins that lack sequence homology with UL42 or PCNA.
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(as it appears on PubMed at http://www.pubmed.gov), where 10882068 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10882068}}
==About this Structure==
==About this Structure==
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[[Category: Processivity]]
[[Category: Processivity]]
[[Category: Sliding clamp]]
[[Category: Sliding clamp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:01:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:18:06 2008''

Revision as of 20:18, 30 June 2008

Image:1dml.png

Template:STRUCTURE 1dml

CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL

Template:ABSTRACT PUBMED 10882068

About this Structure

1DML is a Protein complex structure of sequences from Human herpesvirus 1. Full crystallographic information is available from OCA.

Reference

The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase., Zuccola HJ, Filman DJ, Coen DM, Hogle JM, Mol Cell. 2000 Feb;5(2):267-78. PMID:10882068

Page seeded by OCA on Mon Jun 30 23:18:06 2008

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