1bkr: 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:1bkr.gif|left|200px]]
{{Seed}}
[[Image:1bkr.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bkr|  PDB=1bkr  |  SCENE=  }}  
{{STRUCTURE_1bkr|  PDB=1bkr  |  SCENE=  }}  


'''CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN AT 1.1 ANGSTROM RESOLUTION'''
===CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN AT 1.1 ANGSTROM RESOLUTION===




==Overview==
<!--
BACKGROUND: The actin-binding site of several cytoskeletal proteins is comprised of two calponin homology (CH) domains in a tandem arrangement. As a single copy, the CH domain is also found in regulatory proteins in muscle and in signal-transduction proteins. The three-dimensional structures of three CH domains are known, but they have not yet clarified the molecular details of the interaction between actin filaments and proteins harbouring CH domains. RESULTS: We have compared the crystal structure of a CH domain from beta-spectrin, which has been refined to 1.1 A resolution, with the two CH domains that constitute the actin-binding region of fimbrin. This analysis has allowed the construction of a structure-based sequence alignment of CH domains that can be used in further comparisons of members of the CH domain family. The study has also improved our understanding of the factors that determine domain architecture, and has led to discussion on the functional differences that seem to exist between subfamilies of CH domains, as regards binding to F-actin. CONCLUSIONS: Our analysis supports biochemical data that implicate a surface centered at the last helix of the N-terminal CH domain as the most probable actin-binding site in cytoskeletal proteins. It is not clear whether the C-terminal domains of the tandem arrangement or the single CH domains have this function alone. This may imply that although the CH domains are homologous and have a conserved structure, they may have evolved to perform different functions.
The line below this paragraph, {{ABSTRACT_PUBMED_9817844}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9817844 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9817844}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: Filamentous actin-binding domain]]
[[Category: Filamentous actin-binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:38:25 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:19:00 2008''

Revision as of 16:19, 30 June 2008

File:1bkr.png

Template:STRUCTURE 1bkr

CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN AT 1.1 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 9817844

About this Structure

1BKR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural comparisons of calponin homology domains: implications for actin binding., Banuelos S, Saraste M, Djinovic Carugo K, Structure. 1998 Nov 15;6(11):1419-31. PMID:9817844

Page seeded by OCA on Mon Jun 30 19:19:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bkr&oldid=578244"