1cun: Difference between revisions

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[[Image:1cun.~~gif~~|left|200px]]

[[Image:1cun.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN~~'''~~

===CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10481916}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10481916 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural protein]]

[[Category: Two repeats of spectrin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:07:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:23:35 2008''

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-[[Image:1cun.gif|left|200px]]
+{{Seed}}
+[[Image:1cun.png|left|200px]]
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 {{STRUCTURE_1cun|  PDB=1cun  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10481916}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10481916 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10481916}}
 ==About this Structure==
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 [[Category: Structural protein]]
 [[Category: Two repeats of spectrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:07:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:23:35 2008''