1cun
From Proteopedia
(New page: 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=" | + | [[Image:1cun.gif|left|200px]]<br /><applet load="1cun" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cun, resolution 2.00Å" /> | caption="1cun, resolution 2.00Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Grum, V L.]] |
[[Category: Li, D.]] | [[Category: Li, D.]] | ||
| - | [[Category: MacDonald, R | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:52 2008'' |
Revision as of 10:09, 21 February 2008
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CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN
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.
About this Structure
1CUN is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Structures of two repeats of spectrin suggest models of flexibility., Grum VL, Li D, MacDonald RI, Mondragon A, Cell. 1999 Aug 20;98(4):523-35. PMID:10481916
Page seeded by OCA on Thu Feb 21 12:09:52 2008
