1yu8: Difference between revisions

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New page: left|200px<br /><applet load="1yu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yu8, resolution 1.45Å" /> '''Crystal Structure of...
 
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[[Image:1yu8.gif|left|200px]]<br /><applet load="1yu8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1yu8.gif|left|200px]]<br /><applet load="1yu8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1yu8, resolution 1.45&Aring;" />
caption="1yu8, resolution 1.45&Aring;" />
'''Crystal Structure of the R37A Mutant of Villin Headpiece'''<br />
'''Crystal Structure of the R37A Mutant of Villin Headpiece'''<br />


==Overview==
==Overview==
Villin-type headpiece domains are approximately 70 amino acid modular, motifs found at the C terminus of a variety of actin, cytoskeleton-associated proteins. The headpiece domain of villin, a, protein found in the actin bundles of the brush border epithelium, is of, interest both as a compact F-actin binding domain and as a model folded, protein. We have determined the high-resolution crystal structures of, chicken villin headpiece (HP67) at 1.4 A resolution as well as two, mutants, R37A and W64Y, at 1.45 and 1.5 A resolution, respectively., Replacement of R37 causes a 5-fold reduction in F-actin binding affinity, in sedimentation assays. Replacement of W64 results in a much more drastic, reduction in F-actin binding affinity without significant changes in, headpiece structure or stability. The detailed comparison of these crystal, structures with each other and to our previously determined NMR structures, of HP67 and the 35-residue autonomously folding subdomain in villin, headpiece, HP35, provides the details of the headpiece fold and further, defines the F-actin binding site of villin-type headpiece domains.
Villin-type headpiece domains are approximately 70 amino acid modular motifs found at the C terminus of a variety of actin cytoskeleton-associated proteins. The headpiece domain of villin, a protein found in the actin bundles of the brush border epithelium, is of interest both as a compact F-actin binding domain and as a model folded protein. We have determined the high-resolution crystal structures of chicken villin headpiece (HP67) at 1.4 A resolution as well as two mutants, R37A and W64Y, at 1.45 and 1.5 A resolution, respectively. Replacement of R37 causes a 5-fold reduction in F-actin binding affinity in sedimentation assays. Replacement of W64 results in a much more drastic reduction in F-actin binding affinity without significant changes in headpiece structure or stability. The detailed comparison of these crystal structures with each other and to our previously determined NMR structures of HP67 and the 35-residue autonomously folding subdomain in villin headpiece, HP35, provides the details of the headpiece fold and further defines the F-actin binding site of villin-type headpiece domains.


==About this Structure==
==About this Structure==
1YU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YU8 OCA].  
1YU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU8 OCA].  


==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Guo, H.C.]]
[[Category: Guo, H C.]]
[[Category: Head, J.F.]]
[[Category: Head, J F.]]
[[Category: McKnight, C.J.]]
[[Category: McKnight, C J.]]
[[Category: Meng, J.]]
[[Category: Meng, J.]]
[[Category: Vardar, D.]]
[[Category: Vardar, D.]]
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[[Category: alpha helix]]
[[Category: alpha helix]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:09 2008''