1mb8: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /> <applet load="1mb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mb8, resolution 2.15Å" /> '''Crystal Structure o...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1mb8.gif|left|200px]]<br />
[[Image:1mb8.gif|left|200px]]<br /><applet load="1mb8" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mb8" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mb8, resolution 2.15&Aring;" />
caption="1mb8, resolution 2.15&Aring;" />
'''Crystal Structure of the actin binding domain of plectin'''<br />
'''Crystal Structure of the actin binding domain of plectin'''<br />


==Overview==
==Overview==
Plectin is a widely expressed cytoskeletal linker. Here we report the, crystal structure of the actin binding domain of plectin and show that, this region is sufficient for interaction with F-actin or the cytoplasmic, region of integrin alpha6beta4. The structure is formed by two calponin, homology domains arranged in a closed conformation. We show that binding, to F-actin induces a conformational change in plectin that is inhibited by, an engineered interdomain disulfide bridge. A two-step induced fit, mechanism involving binding and subsequent domain rearrangement is, proposed. In contrast, interaction with integrin alpha6beta4 occurs in a, closed conformation. Competitive binding of plectin to F-actin and, integrin alpha6beta4 may rely on the observed alternative binding, mechanisms and involve both allosteric and steric factors.
Plectin is a widely expressed cytoskeletal linker. Here we report the crystal structure of the actin binding domain of plectin and show that this region is sufficient for interaction with F-actin or the cytoplasmic region of integrin alpha6beta4. The structure is formed by two calponin homology domains arranged in a closed conformation. We show that binding to F-actin induces a conformational change in plectin that is inhibited by an engineered interdomain disulfide bridge. A two-step induced fit mechanism involving binding and subsequent domain rearrangement is proposed. In contrast, interaction with integrin alpha6beta4 occurs in a closed conformation. Competitive binding of plectin to F-actin and integrin alpha6beta4 may rely on the observed alternative binding mechanisms and involve both allosteric and steric factors.


==Disease==
==Disease==
Line 11: Line 10:


==About this Structure==
==About this Structure==
1MB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MB8 OCA].  
1MB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MB8 OCA].  


==Reference==
==Reference==
Line 17: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Pereda, J.M.de.]]
[[Category: Pereda, J M.de.]]
[[Category: actin binding domain]]
[[Category: actin binding domain]]
[[Category: calponin homology domain]]
[[Category: calponin homology domain]]
Line 24: Line 23:
[[Category: integrin beta4 hemidesmosomes]]
[[Category: integrin beta4 hemidesmosomes]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:09:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:26 2008''