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PDBsum entry 1d0r
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Hormone/growth factor
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PDB id
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1d0r
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Authors
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X.Chang,
D.Keller,
S.Bjorn,
J.J.Led.
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Ref.
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MAGN RESON CHEM, 2001,
39,
477-483.
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Secondary reference #1
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Title
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Nmr studies of the aggregation of glucagon-Like peptide-1: formation of a symmetric helical dimer.
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Authors
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X.Chang,
D.Keller,
S.I.O'Donoghue,
J.J.Led.
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Ref.
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FEBS Lett, 2002,
515,
165-170.
[DOI no: ]
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PubMed id
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Figure 3.
Fig. 3. Summary of sequential and medium-range NOE
connectivities, and schematic representation of the ^1H[α]
chemical shift index (CSI) of (a) monomeric GLP-1 and (b)
aggregated GLP-1. In both cases the sample (1.4 mM, pH 2.5, 300
K) was dissolved in H[2]O with 35% TFE. The observed NOE
connectivities are indicated by bars connecting the two involved
residues, and the intensities of the NOEs are indicated by the
thickness of the bars. The CSIs were calculated according to
Wishart et al. [36]. Slowly exchanging backbone amide protons
are indicated by filled circles (●).
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Figure 5.
Fig. 5. Models for the coiled coil dimer of GLP-1. a:
Helical wheel representation with the terminal residues H1 and
R30 excluded. b: Side-chain hydrogen bond between the carboxylic
acids of the two D9 that may impart the parallel orientation of
the coiled coil. c: Interhelical packing model of the coiled
coil showing the back bone and the C[β] carbons of a and d
residues (prepared using MOLMOL [38]).
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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