PMID- 2646637
OWN - NLM
STAT- MEDLINE
DCOM- 19890413
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 86
IP  - 5
DP  - 1989 Mar
TI  - Sequence-specific 1H-NMR assignments and identification of two small antiparallel 
      beta-sheets in the solution structure of recombinant human transforming growth 
      factor alpha.
PG  - 1519-23
AB  - Transforming growth factor alpha (TGF alpha) is a small mitogenic protein with 
      about 35% sequence identity with epidermal growth factor (EGF). TGF alpha-like 
      proteins have been proposed to play a role in oncogenesis and wound healing. This 
      report describes sequence-specific 1H-NMR resonance assignments for recombinant 
      human TGF alpha (hTGF alpha). These assignments provide the basis for 
      interpreting NMR data which demonstrate that the solution structure of hTGF alpha 
      includes an antiparallel beta-sheet involving residues Gly-19 to Leu-24 and 
      Lys-29 to Cys-34 and a second, smaller, antiparallel beta-sheet involving 
      residues Tyr-38 and Val-39 and His-45 and Ala-46. These data, together with 
      constraints imposed by the disulfide bonds, are combined to construct a molecular 
      model of the polypeptide chain fold for residues Cys-8 to Ala-46. The resulting 
      structure is similar to that of mouse and human EGF. Human TGF alpha and mouse 
      EGF, however, differ with respect to their structural dynamics, since amide 
      proton/deuteron exchange is much faster for hTGF alpha than for mouse EGF at pH 
      3.5.
FAU - Montelione, G T
AU  - Montelione GT
AD  - Biophysics Research Division, University of Michigan, Ann Arbor 48109.
FAU - Winkler, M E
AU  - Winkler ME
FAU - Burton, L E
AU  - Burton LE
FAU - Rinderknecht, E
AU  - Rinderknecht E
FAU - Sporn, M B
AU  - Sporn MB
FAU - Wagner, G
AU  - Wagner G
LA  - eng
GR  - 1GM38608-01A1/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Recombinant Proteins)
RN  - 0 (Solutions)
RN  - 76057-06-2 (Transforming Growth Factors)
RN  - 7YNJ3PO35Z (Hydrogen)
SB  - IM
MH  - Escherichia coli/genetics
MH  - Humans
MH  - Hydrogen
MH  - Magnetic Resonance Spectroscopy/methods
MH  - Protein Conformation
MH  - *Recombinant Proteins
MH  - Solutions
MH  - *Transforming Growth Factors/genetics
PMC - PMC286729
EDAT- 1989/03/01 00:00
MHDA- 1989/03/01 00:01
PMCR- 1989/09/01
CRDT- 1989/03/01 00:00
PHST- 1989/03/01 00:00 [pubmed]
PHST- 1989/03/01 00:01 [medline]
PHST- 1989/03/01 00:00 [entrez]
PHST- 1989/09/01 00:00 [pmc-release]
AID - 10.1073/pnas.86.5.1519 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1989 Mar;86(5):1519-23. doi: 10.1073/pnas.86.5.1519.