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Growth factor PDB-id
 1dzc
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131 a.a. *

* Residue conservation analysis
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PDB id: 1dzc
Name: Growth factor
Title: High resolution structure of acidic fibroblast growth factor. Mutant fgf-4-ala-(23-154), 24 nmr structures

Structure:		 Acidic fibroblast growth factor. Chain: a. Fragment: residues 23-154. Engineered: yes

Source: 		Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:
P05230 (FGF1_HUMAN) Pfam  
Seq: 155 a.a.
Struc: 131 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Resolution: 		not givenÅ

NMR structure: 		24 models

Authors: 		R.M.Lozano,A.Pineda-Lucena,C.Gonzalez,M.A.Jimenez,P.Cuevas, M.Redondo-Horcajo,J.M.Sanz,M.Rico,G.Gimenez-Gallego

Key ref:
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: 10819962] [DOI: 10.1021/bi992544n]

Date: 		24-Feb-00

Release date: 		16-Mar-00

Related entries: 		2afg
1axm
2axm
1rml
1dzd
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    Key reference    
 
 
DOI no: 10.1021/bi992544n Biochemistry 39:4982-4993 (2000)
PubMed id: 10819962  
 
 
1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor.
R.M.Lozano, A.Pineda-Lucena, C.Gonzalez, M.Angeles Jiménez, P.Cuevas, M.Redondo-Horcajo, J.M.Sanz, M.Rico, G.Giménez-Gallego.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference
  PubMed id Reference
18788994 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.
  J Ocul Pharmacol Ther, 24, 445-451.  
18000664 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.
  Appl Microbiol Biotechnol, 77, 1015-1022.  
17573954 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.
  Hepatol Res, 37, 836-844.  
17823117 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.
  J Biol Chem, 282, 31852-31864.  
16995857 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.
  FEBS J, 273, 4716-4727.
PDB code: 2erm
12676958 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.
  J Biol Chem, 278, 21774-21781.
PDB code: 1hkn
11847269 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.
  Protein Sci, 11, 459-466.
PDB codes: 1k5u 1k5v
12067496 P.Cuevas, F.Carceller, and G.Giménez-Gallego (2001).
Fibroblast growth factors in myocardial ischemia / reperfusion injury and ischemic preconditioning.
  J Cell Mol Med, 5, 132-142.  
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.