1f3m
From Proteopedia
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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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, resolution 2.3Å | |||||||
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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
Page seeded by OCA on Thu Mar 20 11:03:55 2008
Categories: Homo sapiens | Single protein | Eck, M J. | Harrison, S C. | Lei, M. | Lu, W. | Mayer, B J. | Meng, W. | Parrini, M-C. | IOD | Autoinhibitory fragment | Homodimer | Kinase domain