2pbd: Difference between revisions

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[[Image:2pbd.~~jpg~~|left|200px]]

[[Image:2pbd.png|left|200px]]

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~~'''~~Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*~~'''~~

===Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*===

~~==Overview==~~

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~~Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin~~-~~actin complexes constitute the largest fraction of polymerization~~-~~competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments.~~ The ~~molecular bases of~~ this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the ~~binding of profilin-actin simultaneously to this poly-Pro and~~ to the ~~G-actin-binding~~ (~~GAB~~) ~~domain of VASP. The actin monomer bound at the GAB domain~~ is ~~proposed to be in position to join the barbed end of~~ the ~~growing filament concurrently with the release of profilin~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17914456}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17914456 is the PubMed ID number.

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==About this Structure==

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[[Category: Ternary complex]]

[[Category: Vasp]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 12~~:46:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:38:28 2008''

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-[[Image:2pbd.jpg|left|200px]]
+{{Seed}}
+[[Image:2pbd.png|left|200px]]
 <!--
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 {{STRUCTURE_2pbd|  PDB=2pbd  |  SCENE=  }}
-'''Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*'''
+===Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*===
-==Overview==
+<!--
-Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin-actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin-actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin.
+The line below this paragraph, {{ABSTRACT_PUBMED_17914456}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17914456 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17914456}}
 ==About this Structure==
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 [[Category: Ternary complex]]
 [[Category: Vasp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:46:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:38:28 2008''