2f2o: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2f2o.gif|left|200px]]
{{Seed}}
[[Image:2f2o.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f2o|  PDB=2f2o  |  SCENE=  }}  
{{STRUCTURE_2f2o|  PDB=2f2o  |  SCENE=  }}  


'''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode'''
===Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode===




==Overview==
<!--
Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.
The line below this paragraph, {{ABSTRACT_PUBMED_16411749}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16411749 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16411749}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Calmodulin]]
[[Category: Calmodulin]]
[[Category: Ef-hand]]
[[Category: Ef-hand]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:23:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:39:56 2008''

Revision as of 13:39, 27 July 2008

File:2f2o.png

Template:STRUCTURE 2f2o

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Template:ABSTRACT PUBMED 16411749

About this Structure

2F2O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode., Ye Q, Li X, Wong A, Wei Q, Jia Z, Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749

Page seeded by OCA on Sun Jul 27 16:39:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2f2o&oldid=656271"