4p3e: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
[[4p3e]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3E OCA]. | [[4p3e]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3E OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:024700861</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:024700861</ref><references group="xtra"/><references/> | ||
[[Category: Human]] | |||
[[Category: Grotwinkel, J T.]] | [[Category: Grotwinkel, J T.]] | ||
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: Wild, K.]] | [[Category: Wild, K.]] | ||
[[Category: Srpsrp rnasrp19srp68]] | [[Category: Srpsrp rnasrp19srp68]] | ||
Revision as of 06:12, 23 April 2014
Structure of the human SRP S domain
Template:ABSTRACT PUBMED 24700861
Function
[SRP68_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. [SRP19_HUMAN] Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
About this Structure
4p3e is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA.
Reference
- Grotwinkel JT, Wild K, Segnitz B, Sinning I. SRP RNA remodeling by SRP68 explains its role in protein translocation. Science. 2014 Apr 4;344(6179):101-4. doi: 10.1126/science.1249094. PMID:24700861 doi:https://dx.doi.org/10.1126/science.1249094
