PMID- 12049637
OWN - NLM
STAT- MEDLINE
DCOM- 20020815
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 364
IP  - Pt 3
DP  - 2002 Jun 15
TI  - Solution structure and backbone dynamics of human epidermal-type fatty 
      acid-binding protein (E-FABP).
PG  - 725-37
AB  - Human epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of 
      intracellular 14-15 kDa lipid-binding proteins, whose functions have been 
      associated with fatty acid signalling, cell growth, regulation and 
      differentiation. As a contribution to understanding the structure-function 
      relationship, we report in the present study features of its solution structure 
      and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional 
      high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human 
      E-FABP, the 1H and 15N resonance assignments were completed. On the basis of 2008 
      distance restraints, the three-dimensional solution structure of human E-FABP was 
      subsequently obtained (backbone atom root-mean-square deviation of 0.92+/-0.11 A; 
      where 1 A=0.1 nm), consisting mainly of 10 anti-parallel beta-strands that form a 
      beta-barrel structure. 15N relaxation experiments (T1, T2 and heteronuclear 
      nuclear Overhauser effects) at 500, 600 and 800 MHz provided information on the 
      internal dynamics of the protein backbone. Nearly all non-terminal backbone amide 
      groups showed order parameters S(2)>0.8, with an average value of 0.88+/-0.04, 
      suggesting a uniformly low backbone mobility in the nanosecond-to-picosecond time 
      range. Moreover, hydrogen/deuterium exchange experiments indicated a direct 
      correlation between the stability of the hydrogen-bonding network in the 
      beta-sheet structure and the conformational exchange in the 
      millisecond-to-microsecond time range. The features of E-FABP backbone dynamics 
      elaborated in the present study differ markedly from those of the 
      phylogenetically closely related heart-type FABP and the more distantly related 
      ileal lipid-binding protein, implying a strong interdependence with the overall 
      protein stability and possibly also with the ligand-binding affinity for members 
      of the lipid-binding protein family.
FAU - Gutierrez-Gonzalez, Luis H
AU  - Gutierrez-Gonzalez LH
AD  - Institut fur Biophysikalische Chemie, Johann Wolfgang Goethe-Universitat 
      Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany.
FAU - Ludwig, Christian
AU  - Ludwig C
FAU - Hohoff, Carsten
AU  - Hohoff C
FAU - Rademacher, Martin
AU  - Rademacher M
FAU - Hanhoff, Thorsten
AU  - Hanhoff T
FAU - Ruterjans, Heinz
AU  - Ruterjans H
FAU - Spener, Friedrich
AU  - Spener F
FAU - Lucke, Christian
AU  - Lucke C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Carrier Proteins)
RN  - 0 (FABP5 protein, human)
RN  - 0 (FABP7 protein, human)
RN  - 0 (Fatty Acid-Binding Protein 7)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Fatty Acids)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Solutions)
RN  - 0 (Tumor Suppressor Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Carrier Proteins/*chemistry/metabolism
MH  - Fatty Acid-Binding Protein 7
MH  - Fatty Acid-Binding Proteins
MH  - Fatty Acids/metabolism
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Neoplasm Proteins
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Solutions
MH  - *Tumor Suppressor Proteins
PMC - PMC1222622
EDAT- 2002/06/07 10:00
MHDA- 2002/08/16 10:01
PMCR- 2002/12/15
CRDT- 2002/06/07 10:00
PHST- 2002/06/07 10:00 [pubmed]
PHST- 2002/08/16 10:01 [medline]
PHST- 2002/06/07 10:00 [entrez]
PHST- 2002/12/15 00:00 [pmc-release]
AID - BJ20020039 [pii]
AID - 10.1042/BJ20020039 [doi]
PST - ppublish
SO  - Biochem J. 2002 Jun 15;364(Pt 3):725-37. doi: 10.1042/BJ20020039.