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2h4p
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ment-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |GENE= ment-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2h4q|2H4Q]], [[2h4r|2H4R]], [[2h4s|2H4S]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4p OCA], [http://www.ebi.ac.uk/pdbsum/2h4p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h4p RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:25:24 2008'' |
Revision as of 00:25, 31 March 2008
| |||||||
| , resolution 1.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | ment-1 (Gallus gallus) | ||||||
| Related: | 2H4Q, 2H4R, 2H4S
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of wildtype MENT in the cleaved conformation
Overview
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. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.
About this Structure
2H4P is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation., McGowan S, Buckle AM, Irving JA, Ong PC, Bashtannyk-Puhalovich TA, Kan WT, Henderson KN, Bulynko YA, Popova EY, Smith AI, Bottomley SP, Rossjohn J, Grigoryev SA, Pike RN, Whisstock JC, EMBO J. 2006 Jul 12;25(13):3144-55. Epub 2006 Jun 29. PMID:16810322
Page seeded by OCA on Mon Mar 31 03:25:24 2008
