3nhc
From Proteopedia
(Difference between revisions)
m (Protected "3nhc" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
[[Image:3nhc.png|left|200px]] | [[Image:3nhc.png|left|200px]] | ||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_3nhc", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_3nhc| PDB=3nhc | SCENE= }} | {{STRUCTURE_3nhc| PDB=3nhc | SCENE= }} | ||
===GYMLGS segment 127-132 from human prion with M129=== | ===GYMLGS segment 127-132 from human prion with M129=== | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, {{ABSTRACT_PUBMED_20685658}}, adds the Publication Abstract to the page | ||
- | (as it appears on PubMed at http://www.pubmed.gov), where 20685658 is the PubMed ID number. | ||
- | --> | ||
{{ABSTRACT_PUBMED_20685658}} | {{ABSTRACT_PUBMED_20685658}} | ||
==About this Structure== | ==About this Structure== | ||
- | [[3nhc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHC OCA]. | + | [[3nhc]] is a 2 chain structure of [[Prion]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHC OCA]. |
+ | |||
+ | ==See Also== | ||
+ | *[[Prion|Prion]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020685658</ref><references group="xtra"/> |
[[Category: Apostol, M I.]] | [[Category: Apostol, M I.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
+ | [[Category: Amyloid-like protofibril]] | ||
+ | [[Category: Protein fibril]] |
Revision as of 09:56, 25 July 2012
Contents |
GYMLGS segment 127-132 from human prion with M129
Template:ABSTRACT PUBMED 20685658
About this Structure
3nhc is a 2 chain structure of Prion. Full crystallographic information is available from OCA.
See Also
Reference
- Apostol MI, Sawaya MR, Cascio D, Eisenberg D. Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 2010 Sep 24;285(39):29671-5. Epub 2010 Aug 4. PMID:20685658 doi:10.1074/jbc.C110.158303