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PDBsum entry 1dzc
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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1h nmr structural characterization of a nonmitogenic, Vasodilatory, Ischemia-Protector and neuromodulatory acidic fibroblast growth factor.
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Authors
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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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Ref.
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Biochemistry, 2000,
39,
4982-4993.
[DOI no: ]
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PubMed id
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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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