2MD8

NMR structure of Sp140 PHD finger cis conformer

Summary for 2MD8

• Entry DOI: 10.2210/pdb2md8/pdb
• Related: 2MD7
• NMR Information: BMRB: 19473
• Descriptor: Nuclear body protein SP140, ZINC ION (2 entities in total)
• Functional Keywords: phd finger, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13342
• Total number of polymer chains: 1
• Total formula weight: 6567.18

Authors

Zucchelli, C.,Quilici, G.,Musco, G. (deposition date: 2013-09-02, release date: 2013-11-13, Last modification date: 2024-11-27)

Primary citation

Zucchelli, C.,Tamburri, S.,Quilici, G.,Palagano, E.,Berardi, A.,Saare, M.,Peterson, P.,Bachi, A.,Musco, G.
Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1.
Febs J., 281:216-231, 2014

PubMed Abstract: Sp140 is a nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. The presence of several chromatin related modules such as plant homeodomain (PHD), bromodomain and SAND domain suggests a role in chromatin-mediated regulation of gene expression; however, its real function is still elusive. Herein we present the solution structure of Sp140-PHD finger and investigate its role as epigenetic reader in vitro. Sp140-PHD presents an atypical PHD finger fold which does not bind to histone H3 tails but is recognized by peptidylprolyl isomerase Pin1. Pin1 specifically binds to a phosphopeptide corresponding to the L3 loop of Sp140-PHD and catalyzes cis-trans isomerization of a pThr-Pro bond. Moreover co-immunoprecipitation experiments demonstrate FLAG-Sp140 interaction with endogenous Pin1 in vivo. Overall these data include Sp140 in the list of the increasing number of Pin1 binders and expand the regulatory potential of PHD fingers as versatile structural platforms for diversified interactions.

PubMed: 24267382
DOI: 10.1111/febs.12588

Experimental method

SOLUTION NMR