1f3m: Difference between revisions
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[[Image:1f3m.gif|left|200px]] | [[Image:1f3m.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1''' | {{Structure | ||
|PDB= 1f3m |SIZE=350|CAPTION= <scene name='initialview01'>1f3m</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F3M is a [ | 1F3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3M OCA]. | ||
==Reference== | ==Reference== | ||
Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch., Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC, Cell. 2000 Aug 4;102(3):387-97. PMID:[http:// | Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch., Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC, Cell. 2000 Aug 4;102(3):387-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10975528 10975528] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: kinase domain]] | [[Category: kinase domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:55 2008'' | ||
Revision as of 09:04, 20 March 2008
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| 1f3m, resolution 2.3Å | |||||||||||||
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| Ligands: | IOD | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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).
About this Structure
1F3M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch., Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC, Cell. 2000 Aug 4;102(3):387-97. PMID:10975528
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