1a8y
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1a8y.gif|left|200px]] | [[Image:1a8y.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1a8y", 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_1a8y| PDB=1a8y | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION''' | '''CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION''' | ||
| Line 31: | Line 28: | ||
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
[[Category: Wesson, C R.]] | [[Category: Wesson, C R.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[Category: Calsequestrin]] |
| - | [[Category: | + | [[Category: Rabbit skeletal muscle]] |
| - | [[Category: | + | [[Category: Sarcoplasmic reticulum]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:59:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:59, 2 May 2008
CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION
Overview
Calsequestrin, the major Ca2+ storage protein of muscle, coordinately binds and releases 40-50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. We have determined the structure of rabbit skeletal muscle calsequestrin. Three very negative thioredoxin-like domains surround a hydrophilic center. Each monomer makes two extensive dimerization contacts, both of which involve the approach of many negative groups. This structure suggests a mechanism by which calsequestrin may achieve high capacity Ca2+ binding. The suggested mechanism involves Ca2+-induced collapse of the three domains and polymerization of calsequestrin monomers arising from three factors: N-terminal arm exchange, helix-helix contacts and Ca2+ cross bridges. This proposed structure-based mechanism accounts for the observed coupling of high capacity Ca2+ binding with protein precipitation.
About this Structure
1A8Y is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum., Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH, Nat Struct Biol. 1998 Jun;5(6):476-83. PMID:9628486 Page seeded by OCA on Fri May 2 09:59:37 2008
