2vh4: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh4 OCA], [http://www.ebi.ac.uk/pdbsum/2vh4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vh4 RCSB]</span> | |||
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[[Category: Whisstock, J C.]] | [[Category: Whisstock, J C.]] | ||
[[Category: Zhang, Q.]] | [[Category: Zhang, Q.]] | ||
[[Category: hydrolase inhibitor]] | [[Category: hydrolase inhibitor]] | ||
[[Category: latent conformation | [[Category: serpin,c sheet polymer,latent conformation]] | ||
''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 05:12:12 2008'' | ||
Revision as of 05:12, 31 March 2008
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| , resolution 2.45Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A LOOP C-SHEET SERPIN POLYMER
OverviewOverview
In this study, we report the X-ray crystal structure of an N-terminally truncated variant of the bacterial serpin, tengpin (tengpinDelta42). Our data reveal that tengpinDelta42 adopts a variation of the latent conformation in which the reactive center loop is hyperinserted into the A beta-sheet and removed from the vicinity of the C-sheet. This conformational change leaves the C beta-sheet completely exposed and permits antiparallel edge-strand interactions between the exposed portion of the reactive center loop of one molecule and strand s2C of the C beta-sheet of the neighboring molecule in the crystal lattice. Our structural data thus reveal that tengpinDelta42 forms a loop C-sheet polymer in the crystal lattice. In vivo serpins have a propensity to misfold and form long-chain polymers, a process that underlies serpinopathies such as emphysema, thrombosis and dementia. Native serpins are thought to polymerize via a loop A-sheet mechanism. However, studies on plasminogen activator inhibitor 1 and the S49P variant of human neuroserpin reveal that the latent form of these molecules can also polymerize. Polymerization of latent neuroserpin may be important for the development of familial encephalopathy with neuroserpin inclusion bodies. Our structural data provide a possible mechanism for polymerization by latent serpins.
About this StructureAbout this Structure
2VH4 is a Single protein structure of sequence from Thermoanaerobacter tengcongensis. Full crystallographic information is available from OCA.
ReferenceReference
A structural basis for loop C-sheet polymerization in serpins., Zhang Q, Law RH, Bottomley SP, Whisstock JC, Buckle AM, J Mol Biol. 2008 Mar 7;376(5):1348-59. Epub 2008 Jan 3. PMID:18234218
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