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A small protein inhibits proliferating cell nuclear antigen by breaking the DNA clamp. Title A small protein inhibits proliferating cell nuclear antigen by breaking the DNA clamp. Publication Type Journal Article Year of Publication 2016 Authors Altieri, AS, Ladner, JE, Li, Z, Robinson, H, Sallman, ZF, Marino, JP, Kelman, Z Journal Nucleic Acids Res Volume 44 Issue 13 Pagination 6232-41 Date Published 2016 Jul 27 ISSN 1362-4962 Abstract Proliferating cell nuclear antigen (PCNA) forms a trimeric ring that encircles duplex DNA and acts as an anchor for a number of proteins involved in DNA metabolic processes. PCNA has two structurally similar domains (I and II) linked by a long loop (inter-domain connector loop, IDCL) on the outside of each monomer of the trimeric structure that makes up the DNA clamp. All proteins that bind to PCNA do so via a PCNA-interacting peptide (PIP) motif that binds near the IDCL. A small protein, called TIP, binds to PCNA and inhibits PCNA-dependent activities although it does not contain a canonical PIP motif. The X-ray crystal structure of TIP bound to PCNA reveals that TIP binds to the canonical PIP interaction site, but also extends beyond it through a helix that relocates the IDCL. TIP alters the relationship between domains I and II within the PCNA monomer such that the trimeric ring structure is broken, while the individual domains largely retain their native structure. Small angle X-ray scattering (SAXS) confirms the disruption of the PCNA trimer upon addition of the TIP protein in solution and together with the X-ray crystal data, provides a structural basis for the mechanism of PCNA inhibition by TIP. DOI 10.1093/nar/gkw351 Alternate Journal Nucleic Acids Res. PubMed ID 27141962