1f3m: Difference between revisions

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[[Image:1f3m.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1~~'''~~

===CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1===

~~==Overview==~~

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The ~~p21-activated kinases (PAKs)~~, ~~stimulated by binding with GTP-liganded forms of Cdc42 or Rac~~, ~~modulate cytoskeletal actin assembly and activate MAP-kinase pathways. The 2.3 A resolution crystal structure of a complex between~~ the ~~N-terminal autoregulatory fragment and~~ the C-terminal kinase domain of PAK1 shows that GTPase binding will trigger a series of conformational changes, beginning with disruption of a PAK1 dimer and ending with rearrangement of the kinase active site into a catalytically competent state. ~~An inhibitory switch (IS~~) ~~domain, which overlaps the GTPase binding region of PAK1~~, ~~positions a polypeptide segment across~~ the ~~kinase cleft~~. ~~GTPase binding will refold part of the IS domain and unfold the rest. A related switch has been seen in the Wiskott~~-~~Aldrich syndrome protein (WASP).~~

The line below this paragraph, {{ABSTRACT_PUBMED_10975528}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10975528 is the PubMed ID number.

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==About this Structure==

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[[Category: Homodimer]]

[[Category: Kinase domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:51:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:37:19 2008''

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-[[Image:1f3m.gif|left|200px]]
+{{Seed}}
+[[Image:1f3m.png|left|200px]]
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 {{STRUCTURE_1f3m|  PDB=1f3m  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1'''
+===CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1===
-==Overview==
+<!--
-The p21-activated kinases (PAKs), stimulated by binding with GTP-liganded forms of Cdc42 or Rac, modulate cytoskeletal actin assembly and activate MAP-kinase pathways. The 2.3 A resolution crystal structure of a complex between the N-terminal autoregulatory fragment and the C-terminal kinase domain of PAK1 shows that GTPase binding will trigger a series of conformational changes, beginning with disruption of a PAK1 dimer and ending with rearrangement of the kinase active site into a catalytically competent state. An inhibitory switch (IS) domain, which overlaps the GTPase binding region of PAK1, positions a polypeptide segment across the kinase cleft. GTPase binding will refold part of the IS domain and unfold the rest. A related switch has been seen in the Wiskott-Aldrich syndrome protein (WASP).
+The line below this paragraph, {{ABSTRACT_PUBMED_10975528}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10975528 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10975528}}
 ==About this Structure==
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 [[Category: Homodimer]]
 [[Category: Kinase domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:51:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:37:19 2008''