1dx0: Difference between revisions
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==BOVINE PRION PROTEIN RESIDUES 23-230== | ==BOVINE PRION PROTEIN RESIDUES 23-230== | ||
<StructureSection load='1dx0' size='340' side='right' caption='[[1dx0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1dx0' size='340' side='right' caption='[[1dx0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dx0]] is a 1 chain structure | <table><tr><td colspan='2'>[[1dx0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DX0 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dwz|1dwz]], [[1dwy|1dwy]], [[1dx1|1dx1]], [[1ag2|1ag2]], [[1b10|1b10]], [[1qlx|1qlx]], [[1qm0|1qm0]], [[1qm1|1qm1]], [[1qm2|1qm2]], [[1qm3|1qm3]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dwz|1dwz]], [[1dwy|1dwy]], [[1dx1|1dx1]], [[1ag2|1ag2]], [[1b10|1b10]], [[1qlx|1qlx]], [[1qm0|1qm0]], [[1qm1|1qm1]], [[1qm2|1qm2]], [[1qm3|1qm3]]</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=1dx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx0 OCA], [http://pdbe.org/1dx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dx0 RCSB], [http://www.ebi.ac.uk/pdbsum/1dx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dx0 ProSAT]</span></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=1dx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx0 OCA], [http://pdbe.org/1dx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dx0 RCSB], [http://www.ebi.ac.uk/pdbsum/1dx0 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dx0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Billeter, M]] | [[Category: Billeter, M]] | ||
[[Category: Lopez-Garcia, F]] | [[Category: Lopez-Garcia, F]] | ||
Revision as of 07:07, 30 August 2017
BOVINE PRION PROTEIN RESIDUES 23-230BOVINE PRION PROTEIN RESIDUES 23-230
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 PubMedThe NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230), include a globular domain extending from residue 125 to residue 227, a short flexible chain end of residues 228-230, and an N-terminal flexibly disordered "tail" comprising 108 residues for the intact protein and 4 residues for bPrP(121-230), respectively. The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-226, and a short antiparallel beta-sheet comprising the residues 128-131 and 161-164. The best-defined parts of the globular domain are the central portions of the helices 2 and 3, which are linked by the only disulfide bond in bPrP. Significantly increased disorder and mobility is observed for helix 1, the loop 166-172 leading from the beta-strand 2 to helix 2, the end of helix 2 and the following loop, and the last turn of helix 3. Although there are characteristic local differences relative to the conformations of the murine and Syrian hamster prion proteins, the bPrP structure is essentially identical to that of the human prion protein. On the other hand, there are differences between bovine and human PrP in the surface distribution of electrostatic charges, which then appears to be the principal structural feature of the "healthy" PrP form that might affect the stringency of the species barrier for transmission of prion diseases between humans and cattle. NMR structure of the bovine prion protein.,Lopez Garcia F, Zahn R, Riek R, Wuthrich K Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8334-9. PMID:10899999[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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