PMID- 10623549
OWN - NLM
STAT- MEDLINE
DCOM- 20000218
LR  - 20061115
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 295
IP  - 3
DP  - 2000 Jan 21
TI  - NMR structure of the sterol carrier protein-2: implications for the biological 
      role.
PG  - 595-603
AB  - The determination of the NMR structure of the sterol carrier protein-2 (SCP2), 
      analysis of backbone (15)N spin relaxation parameters and NMR studies of 
      nitroxide spin-labeled substrate binding are presented as a new basis for 
      investigations of the mode of action of SCP2. The SCP2 fold is formed by a 
      five-stranded beta-sheet and four alpha-helices. Fatty acid binding to a 
      hydrophobic surface area formed by amino acid residues of the first and third 
      helices, and the beta-sheet, which are all located in the polypeptide segment 
      8-102, was identified with the use of the spin-labeled substrate 16-doxylstearic 
      acid. In the free protein, the lipid-binding site is covered by the C-terminal 
      segment 105-123, suggesting that this polypeptide segment, which carries the 
      peroxisomal targeting signal (PTS1), might be involved in the regulation of 
      ligand binding.
CI  - Copyright 2000 Academic Press.
FAU - Garcia, F L
AU  - Garcia FL
AD  - Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische 
      Hochschule-Honggerberg, Zurich, CH-8093, Switzerland.
FAU - Szyperski, T
AU  - Szyperski T
FAU - Dyer, J H
AU  - Dyer JH
FAU - Choinowski, T
AU  - Choinowski T
FAU - Seedorf, U
AU  - Seedorf U
FAU - Hauser, H
AU  - Hauser H
FAU - Wuthrich, K
AU  - Wuthrich K
LA  - eng
SI  - PDB/1QND
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Carrier Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (sterol carrier proteins)
SB  - IM
MH  - Animals
MH  - Carrier Proteins/chemistry/*metabolism
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Models, Molecular
MH  - *Plant Proteins
MH  - Protein Conformation
MH  - Protein Folding
MH  - Rabbits
EDAT- 2000/01/07 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/07 09:00
PHST- 2000/01/07 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/07 09:00 [entrez]
AID - S0022-2836(99)93355-7 [pii]
AID - 10.1006/jmbi.1999.3355 [doi]
PST - ppublish
SO  - J Mol Biol. 2000 Jan 21;295(3):595-603. doi: 10.1006/jmbi.1999.3355.