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PDBsum entry 1jt5
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protein ligands Protein-protein interface(s) links
Hormone/growth factor PDB id
1jt5

 

 

 

 

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Contents
Protein chains
142 a.a. *
Ligands
SO4 ×4
Waters ×217
* Residue conservation analysis
PDB id:
1jt5
Name: Hormone/growth factor
Title: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 73 replaced by val and val 109 replaced by leu (l73v/v109l)
Structure: Acidic fibroblast growth factor. Chain: a, b. Synonym: heparin-binding growth factor 1, hbgf-1, afgf. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.203     R-free:   0.236
Authors: S.R.Brych,S.I.Blaber,T.M.Logan,M.Blaber
Key ref: S.R.Brych et al. (2001). Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil. Protein Sci, 10, 2587-2599. PubMed id: 11714927
Date:
20-Aug-01     Release date:   19-Dec-01    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05230  (FGF1_HUMAN) -  Fibroblast growth factor 1 from Homo sapiens
Seq:
Struc: 		155 a.a.
142 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 

 
Protein Sci 10:2587-2599 (2001)
PubMed id: 11714927  
 
 
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
S.R.Brych, S.I.Blaber, T.M.Logan, M.Blaber.
 
  ABSTRACT  
 
Human acidic fibroblast growth factor (FGF-1) is a member of the beta-trefoil hyperfamily and exhibits a characteristic threefold symmetry of the tertiary structure. However, evidence of this symmetry is not readily apparent at the level of the primary sequence. This suggests that while selective pressures may exist to retain (or converge upon) a symmetric tertiary structure, other selective pressures have resulted in divergence of the primary sequence during evolution. Using intra-chain and homologue sequence comparisons for 19 members of this family of proteins, we have designed mutants of FGF-1 that constrain a subset of core-packing residues to threefold symmetry at the level of the primary sequence. The consequences of these mutations regarding structure and stability were evaluated using a combination of X-ray crystallography and differential scanning calorimetry. The mutational effects on structure and stability can be rationalized through the characterization of "microcavities" within the core detected using a 1.0A probe radius. The results show that the symmetric constraint within the primary sequence is compatible with a well-packed core and near wild-type stability. However, despite the general maintenance of overall thermal stability, a noticeable increase in non-two-state denaturation follows the increase in primary sequence symmetry. Therefore, properties of folding, rather than stability, may contribute to the selective pressure for asymmetric primary core sequences within symmetric protein architectures.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21173271 J.Lee, and M.Blaber (2011).
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
  Proc Natl Acad Sci U S A, 108, 126-130.
PDB codes: 3o49 3o4a 3o4b 3o4c 3o4d 3ogf 3ol0
21315087 J.Lee, S.I.Blaber, V.K.Dubey, and M.Blaber (2011).
A polypeptide "building block" for the β-trefoil fold identified by "top-down symmetric deconstruction".
  J Mol Biol, 407, 744-763.
PDB code: 3o3q
21152439 J.Feng, M.Li, Y.Huang, and Y.Xiao (2010).
Symmetric key structural residues in symmetric proteins with beta-trefoil fold.
  PLoS One, 5, e14138.  
18421160 E.Honjo, T.Tamada, M.Adachi, R.Kuroki, A.Meher, and M.Blaber (2008).
Mutagenesis of the crystal contact of acidic fibroblast growth factor.
  J Synchrotron Radiat, 15, 285-287.  
18320584 M.Li, Y.Huang, and Y.Xiao (2008).
Effects of external interactions on protein sequence-structure relations of beta-trefoil fold.
  Proteins, 72, 1161-1170.  
17932930 S.Choi, J.Jeon, J.S.Yang, and S.Kim (2008).
Common occurrence of internal repeat symmetry in membrane proteins.
  Proteins, 71, 68-80.  
  17277441 N.Kulahin, V.Kiselyov, A.Kochoyan, O.Kristensen, J.S.Kastrup, V.Berezin, E.Bock, and M.Gajhede (2007).
Structure of rat acidic fibroblast growth factor at 1.4 A resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 65-68.
PDB code: 2j3p
16355415 J.Lee, V.K.Dubey, T.Somasundaram, and M.Blaber (2006).
Conversion of type I 4:6 to 3:5 beta-turn types in human acidic fibroblast growth factor: effects upon structure, stability, folding, and mitogenic function.
  Proteins, 62, 686-697.
PDB codes: 1yto 1z2v 1z4s 2aqz
15632285 J.Kim, J.Lee, S.R.Brych, T.M.Logan, and M.Blaber (2005).
Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.
  Protein Sci, 14, 351-359.
PDB codes: 1pzz 1q03 1q04
16081654 V.K.Dubey, J.Lee, and M.Blaber (2005).
Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: thermodynamic and functional consequences of structural symmetry.
  Protein Sci, 14, 2315-2323.  
15382229 M.J.Bernett, T.Somasundaram, and M.Blaber (2004).
An atomic resolution structure for human fibroblast growth factor 1.
  Proteins, 57, 626-634.
PDB code: 1rg8
14627732 S.R.Brych, J.Kim, T.M.Logan, and M.Blaber (2003).
Accommodation of a highly symmetric core within a symmetric protein superfold.
  Protein Sci, 12, 2704-2718.
PDB codes: 1jy0 1m16 1nzk 1p63
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
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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