2vh4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | |||
==Structure of a loop C-sheet serpin polymer== | |||
<StructureSection load='2vh4' size='340' side='right' caption='[[2vh4]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='2vh4' size='340' side='right' caption='[[2vh4]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vh4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2vh4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cals4 Cals4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VH4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2vh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vh4 RCSB], [http://www.ebi.ac.uk/pdbsum/2vh4 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2vh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vh4 RCSB], [http://www.ebi.ac.uk/pdbsum/2vh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vh4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 9: | Line 10: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vh/2vh4_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vh/2vh4_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 28: | Line 29: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cals4]] | ||
[[Category: Bottomley, S P]] | [[Category: Bottomley, S P]] | ||
[[Category: Buckle, A M]] | [[Category: Buckle, A M]] | ||
Revision as of 23:56, 19 September 2018
Structure of a loop C-sheet serpin polymerStructure of a loop C-sheet serpin polymer
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||