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PDBsum entry 1v6f
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Hormone/growth factor
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PDB id
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1v6f
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Contents |
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* Residue conservation analysis
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PDB id:
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Hormone/growth factor
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Title:
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Solution structure of glia maturation factor-beta from mus musculus
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Structure:
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Glia maturation factor, beta. Chain: a. Fragment: cofilin-adf domian. Synonym: mgmf-beta. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: riken cdna 3110001h22. Other_details: cell-free protein synthesis
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NMR struc:
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20 models
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Authors:
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A.K.Goroncy,T.Kigawa,S.Koshiba,T.Tomizawa,N.Kobayashi,N.Tochio, M.Inoue,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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A.K.Goroncy
et al.
(2009).
NMR solution structures of actin depolymerizing factor homology domains.
Protein Sci,
18,
2384-2392.
PubMed id:
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Date:
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29-Nov-03
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Release date:
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29-May-04
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PROCHECK
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Headers
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References
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Q9CQI3
(GMFB_MOUSE) -
Glia maturation factor beta from Mus musculus
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Seq:
Struc:
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142 a.a.
151 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 4 residue positions (black
crosses)
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Protein Sci
18:2384-2392
(2009)
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PubMed id:
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NMR solution structures of actin depolymerizing factor homology domains.
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A.K.Goroncy,
S.Koshiba,
N.Tochio,
T.Tomizawa,
M.Sato,
M.Inoue,
S.Watanabe,
Y.Hayashizaki,
A.Tanaka,
T.Kigawa,
S.Yokoyama.
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ABSTRACT
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Actin is one of the most conserved proteins in nature. Its assembly and
disassembly are regulated by many proteins, including the family of
actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be
divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin,
twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The
other four classes have drawn much less attention and very few structures have
been reported. This study presents the solution NMR structure of the ADF-H
domain of human HIP-55-drebrin-like protein, the first published structure of a
drebrin-like domain (mammalian), and the first published structure of GMF beta
(mouse). We also determined the structures of mouse GMF gamma, the mouse
coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1.
Although the overall fold of the five domains is similar, some significant
differences provide valuable insights into filamentous actin (F-actin) and
globular actin (G-actin) binding, including the identification of binding
residues on the long central helix. This long helix is stabilized by three or
four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF
gamma contain two additional beta-strands not seen in other ADF-H structures.
The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like
protein is absent and distorted in mouse GMF beta and GMF gamma.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.K.Goroncy,
K.Murayama,
M.Shirouzu,
S.Kuramitsu,
T.Kigawa,
and
S.Yokoyama
(2010).
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
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J Struct Funct Genomics,
11,
247-256.
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A.K.Goroncy,
S.Koshiba,
N.Tochio,
T.Tomizawa,
M.Inoue,
M.Inoue,
S.Watanabe,
T.Harada,
A.Tanaka,
O.Ohara,
T.Kigawa,
and
S.Yokoyama
(2010).
The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein.
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J Struct Funct Genomics,
11,
181-188.
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PDB codes:
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M.Gandhi,
B.A.Smith,
M.Bovellan,
V.Paavilainen,
K.Daugherty-Clarke,
J.Gelles,
P.Lappalainen,
and
B.L.Goode
(2010).
GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation.
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Curr Biol,
20,
861-867.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
