<HashMap><database>biostudies-literature</database><scores/><additional><submitter>McGowan S</submitter><funding>NIGMS NIH HHS</funding><pagination>3144-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1500978</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>25(13)</volume><pubmed_abstract>Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. Thes</pubmed_abstract><journal>The EMBO journal</journal><pubmed_title>X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.</pubmed_title><pmcid>PMC1500978</pmcid><funding_grant_id>R01 GM059118</funding_grant_id><funding_grant_id>GM-59118</funding_grant_id><pubmed_authors>Kan WT</pubmed_authors><pubmed_authors>Bulynko YA</pubmed_authors><pubmed_authors>Rossjohn J</pubmed_authors><pubmed_authors>Ong PC</pubmed_authors><pubmed_authors>Smith AI</pubmed_authors><pubmed_authors>McGowan S</pubmed_authors><pubmed_authors>Irving JA</pubmed_authors><pubmed_authors>Bottomley SP</pubmed_authors><pubmed_authors>Whisstock JC</pubmed_authors><pubmed_authors>Buckle AM</pubmed_authors><pubmed_authors>Henderson KN</pubmed_authors><pubmed_authors>Bashtannyk-Puhalovich TA</pubmed_authors><pubmed_authors>Pike RN</pubmed_authors><pubmed_authors>Grigoryev SA</pubmed_authors><pubmed_authors>Popova EY</pubmed_authors></additional><is_claimable>false</is_claimable><name>X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.</name><description>Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. Thes</description><dates><release>2006-01-01T00:00:00Z</release><publication>2006 Jul</publication><modification>2026-04-29T20:45:07.611Z</modification><creation>2019-03-27T01:45:36Z</creation></dates><accession>S-EPMC1500978</accession><cross_references><pubmed>16810322</pubmed><doi>10.1038/sj.emboj.7601201</doi></cross_references></HashMap>