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PDBsum entry 3v8o
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Structural protein
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PDB id
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3v8o
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PDB id:
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| Name: |
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Structural protein
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Title:
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Human filamin c ig - like domains 4 and 5
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Structure:
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Filamin-c. Chain: a, b. Fragment: domains 4 and 5 (unp residues 569-761). Synonym: fln-c, flnc, abp-280-like protein, abp-l, actin-binding-like protein, filamin-2, gamma-filamin. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: abpl, fln2, flnc. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.80Å
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R-factor:
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0.206
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R-free:
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0.255
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Authors:
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R.Sethi,J.Ylanne
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Key ref:
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R.Sethi
et al.
(2014).
A novel structural unit in the N-terminal region of filamins.
J Biol Chem,
289,
8588-8598.
PubMed id:
DOI:
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Date:
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23-Dec-11
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Release date:
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17-Jul-13
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PROCHECK
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Headers
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References
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Q14315
(FLNC_HUMAN) -
Filamin-C from Homo sapiens
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Seq:
Struc:
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2725 a.a.
193 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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J Biol Chem
289:8588-8598
(2014)
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PubMed id:
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A novel structural unit in the N-terminal region of filamins.
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R.Sethi,
J.Seppälä,
H.Tossavainen,
M.Ylilauri,
S.Ruskamo,
O.T.Pentikäinen,
U.Pentikäinen,
P.Permi,
J.Ylänne.
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ABSTRACT
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Immunoglobulin-like (Ig) domains are a widely expanded superfamily that act as
interaction motifs or as structural spacers in multidomain proteins. Vertebrate
filamins (FLNs), which are multifunctional actin-binding proteins, consist of 24
Ig domains. We have recently discovered that in the C-terminal rod 2 region of
FLN, Ig domains interact with each other forming functional domain pairs, where
the interaction with signaling and transmembrane proteins is mechanically
regulated by weak actomyosin contraction forces. Here, we investigated if there
are similar inter-domain interactions around domain 4 in the N-terminal rod 1
region of FLN. Protein crystal structures revealed a new type of domain
organization between domains 3, 4, and 5. In this module, domains 4 and 5
interact rather tightly, whereas domain 3 has a partially flexible interface
with domain 4. NMR peptide titration experiments showed that within the
three-domain module, domain 4 is capable for interaction with a peptide derived
from platelet glycoprotein Ib. Crystal structures of FLN domains 4 and 5 in
complex with the peptide revealed a typical β sheet augmentation interaction
observed for many FLN ligands. Domain 5 was found to stabilize domain 4, and
this could provide a mechanism for the regulation of domain 4 interactions.
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Links
