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PDBsum entry 1dzc
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* Residue conservation analysis
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PDB id:
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Cell cycle
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Title:
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High resolution structure of acidic fibroblast growth factor. Mutant fgf-4-ala-(24-154), 24 nmr structures
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Structure:
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Fibroblast growth factor 1. Chain: a. Fragment: residues 25-155. Synonym: fgf-1, acidic fibroblast growth factor, afgf, ecgf,hbgf-1, endothelial cell growth factor, heparin-binding growth factor 1. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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24 models
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Authors:
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R.M.Lozano,A.Pineda-Lucena,C.Gonzalez,M.A.Jimenez,P.Cuevas,M.Redondo- Horcajo,J.M.Sanz,M.Rico,G.Gimenez-Gallego
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Key ref:
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R.M.Lozano
et al.
(2000).
1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor.
Biochemistry,
39,
4982-4993.
PubMed id:
DOI:
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Date:
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24-Feb-00
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Release date:
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16-Mar-00
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PROCHECK
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Headers
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References
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P05230
(FGF1_HUMAN) -
Fibroblast growth factor 1 from Homo sapiens
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Seq:
Struc:
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155 a.a.
131 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 3 residue positions (black
crosses)
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DOI no:
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Biochemistry
39:4982-4993
(2000)
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PubMed id:
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1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor.
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R.M.Lozano,
A.Pineda-Lucena,
C.Gonzalez,
M.Angeles Jiménez,
P.Cuevas,
M.Redondo-Horcajo,
J.M.Sanz,
M.Rico,
G.Giménez-Gallego.
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ABSTRACT
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A shortened genetically engineered form of acidic fibroblast growth factor
(aFGF), that includes amino acids 28-154 of the full-length sequence (154
residues) plus Met in substitution of Leu27, does not induce cell division even
though it is recognized by the cell membrane receptor, triggers the early
mitogenic events, and retains the neuromodulatory, vasoactive, and cardio- and
neuroprotective properties of the native full-length molecule. Taken together,
these properties make this truncated aFGF a promising compound in the treatment
of a wide assortment of neurological and cardiovascular pathologies where aFGF
mitogenic activity is dispensable. Differences in biological activities between
the shortened aFGF and the wild-type form have been attributed to lack of
stability, and to the specific amino acid sequence missing at the N-terminus.
Here we show that this shortened aFGF form has a three-dimensional structure
even more stable than the wild-type protein at the mitogenic assay conditions;
that this structure is similar to that of the wild type except at site 1 of
interaction with the cell membrane receptor; that its lack of mitogenic activity
cannot be attributed to the specific missing sequence; and that the vasodilatory
activity of aFGF seems impaired by alterations of the three-dimensional
structure of site 2 of interaction with the cell membrane receptor.
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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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H.Xu,
J.N.Yang,
X.K.Li,
Q.Zheng,
W.Zhao,
Z.J.Su,
and
Y.D.Huang
(2008).
Retina protective effect of acidic fibroblast growth factor after canceling its mitogenic activity.
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J Ocul Pharmacol Ther,
24,
445-451.
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Y.Huang,
Y.Rao,
C.Feng,
Y.Li,
X.Wu,
Z.Su,
J.Xiao,
Y.Xiao,
W.Feng,
and
X.Li
(2008).
High-level expression and purification of Tat-haFGF19-154.
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Appl Microbiol Biotechnol,
77,
1015-1022.
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H.Xu,
G.F.Hai,
J.Z.Xiang,
C.C.Yao,
Q.Zheng,
Q.H.Zhang,
and
H.Hong
(2007).
Protective effect of non-mitogenic human acidic fibroblast growth factor on hepatocyte injury.
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Hepatol Res,
37,
836-844.
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H.Yoon,
G.Laxmikanthan,
J.Lee,
S.I.Blaber,
A.Rodriguez,
J.M.Kogot,
I.A.Scarisbrick,
and
M.Blaber
(2007).
Activation profiles and regulatory cascades of the human kallikrein-related peptidases.
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J Biol Chem,
282,
31852-31864.
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X.Wu,
X.Liu,
Y.Xiao,
Z.Huang,
J.Xiao,
S.Lin,
L.Cai,
W.Feng,
and
X.Li
(2007).
Purification and modification by polyethylene glycol of a new human basic fibroblast growth factor mutant-hbFGF(Ser25,87,92).
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J Chromatogr A,
1161,
51-55.
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A.Canales,
R.Lozano,
B.López-Méndez,
J.Angulo,
R.Ojeda,
P.M.Nieto,
M.Martín-Lomas,
G.Giménez-Gallego,
and
J.Jiménez-Barbero
(2006).
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue.
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FEBS J,
273,
4716-4727.
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PDB code:
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C.Fernández-Tornero,
R.M.Lozano,
M.Redondo-Horcajo,
A.M.Gómez,
J.C.López,
E.Quesada,
C.Uriel,
S.Valverde,
P.Cuevas,
A.Romero,
and
G.Giménez-Gallego
(2003).
Leads for development of new naphthalenesulfonate derivatives with enhanced antiangiogenic activity: crystal structure of acidic fibroblast growth factor in complex with 5-amino-2-naphthalene sulfonate.
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J Biol Chem,
278,
21774-21781.
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PDB code:
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J.Kim,
S.I.Blaber,
and
M.Blaber
(2002).
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor.
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Protein Sci,
11,
459-466.
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PDB codes:
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P.Cuevas,
F.Carceller,
and
G.Giménez-Gallego
(2001).
Fibroblast growth factors in myocardial ischemia / reperfusion injury and ischemic preconditioning.
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J Cell Mol Med,
5,
132-142.
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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
code is
shown on the right.
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Links
