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PDBsum entry 6fd3
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PDB id:
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Transferase
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Title:
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Thiophosphorylated pak3 kinase domain
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Structure:
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Serine/threonine-protein kinase pak 3. Chain: a. Synonym: beta-pak,oligophrenin-3,p21-activated kinase 3,pak-3. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: pak3, ophn3. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.52Å
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R-factor:
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0.176
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R-free:
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0.190
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Authors:
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F.J.Sorrell,D.Wang,F.Von Delft,C.Bountra,A.M.Edwards,J.M.Elkins
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Key ref:
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F.J.Sorrell
et al.
(2019).
Solution structures and biophysical analysis of full-length group A PAKs reveal they are monomeric and auto-inhibited in cis.
Biochem J,
476,
1037-1051.
PubMed id:
DOI:
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Date:
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21-Dec-17
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Release date:
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03-Jan-18
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PROCHECK
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Headers
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References
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O75914
(PAK3_HUMAN) -
Serine/threonine-protein kinase PAK 3 from Homo sapiens
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Seq:
Struc:
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559 a.a.
297 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
Bound ligand (Het Group name = )
corresponds exactly
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name = )
corresponds exactly
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochem J
476:1037-1051
(2019)
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PubMed id:
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Solution structures and biophysical analysis of full-length group A PAKs reveal they are monomeric and auto-inhibited in cis.
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F.J.Sorrell,
L.M.Kilian,
J.M.Elkins.
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ABSTRACT
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The group A p21-activated kinases (PAKs) exist in an auto-inhibited form until
activated by GTPase binding and auto-phosphorylation. In the auto-inhibited
form, a regulatory domain binds to the kinase domain (KD) blocking the binding
of substrates, and CDC42 or Rac binding to the regulatory domain relieves this
auto-inhibition allowing auto-phosphorylation on the KD activation loop. We have
determined the crystal structure of the PAK3 catalytic domain and by small angle
X-ray scattering, the solution-phase structures of full-length inactive PAK1 and
PAK3. The structures reveal a compact but elongated molecular shape that
demonstrates that, together with multiple independent biophysical measurements
and in contrast with previous assumptions, group A PAKs are monomeric both
before and after activation, consistent with an activation mechanism of
cis-auto-inhibition and initial cis-auto-phosphorylation, followed
by transient dimerisation to allow trans-auto-phosphorylation for full
activation, yielding a monomeric active PAK protein.
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Links
