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New page: left|200px<br /><applet load="1cun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cun, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1cun.gif|left|200px]]<br /><applet load="1cun" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1cun.gif|left|200px]]<br /><applet load="1cun" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1cun, resolution 2.00&Aring;" />
caption="1cun, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN'''<br />
'''CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN'''<br />


==Overview==
==Overview==
Spectrin is a vital component of the cytoskeleton, conferring flexibility, on cells and providing a scaffold for a variety of proteins. It is, composed of tandem, antiparallel coiled-coil repeats. We report four, related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution, of two connected repeats of chicken brain alpha-spectrin. In all of the, structures, the linker region between adjacent units is alpha-helical, without breaks, kinks, or obvious boundaries. Two features observed in the, structures are (1) conformational rearrangement in one repeat, resulting, in movement of the position of a loop, and (2) varying degrees of bending, at the linker region. These features form the basis of two different, models of flexibility: a conformational rearrangement and a bending model., These models provide novel atomic details of spectrin flexibility.
Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.


==About this Structure==
==About this Structure==
1CUN 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=1CUN OCA].  
1CUN 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=1CUN OCA].  


==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Grum, V.L.]]
[[Category: Grum, V L.]]
[[Category: Li, D.]]
[[Category: Li, D.]]
[[Category: MacDonald, R.I.]]
[[Category: MacDonald, R I.]]
[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: 2 tandem 3-helix coiled- coils]]
[[Category: 2 tandem 3-helix coiled- coils]]
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[[Category: two repeats of spectrin]]
[[Category: two repeats of spectrin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:46:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:52 2008''