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PDBsum entry 2j5h
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Hormone/growth factor
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PDB id
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2j5h
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Contents |
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* Residue conservation analysis
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PDB id:
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Hormone/growth factor
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Title:
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Nmr analysis of mouse cripto cfc domain
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Structure:
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Teratocarcinoma-derived growth factor. Chain: a. Fragment: cripto domain, residues 96-134. Synonym: cripto, epidermal growth factor-like cripto protein, cripto growth factor. Engineered: yes. Other_details: three disulfide bridges
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Source:
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Synthetic: yes. Mus musculus. Mouse. Organism_taxid: 10090
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NMR struc:
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10 models
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Authors:
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L.Calvanese,A.Saporito,D.Marasco,G.D'Auria,G.Minchiotti,C.Pedone, L.Paolillo,L.Falcigno,M.Ruvo
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Key ref:
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L.Calvanese
et al.
(2006).
Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala.
J Med Chem,
49,
7054-7062.
PubMed id:
DOI:
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Date:
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18-Sep-06
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Release date:
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02-Oct-06
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PROCHECK
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Headers
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References
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P51865
(TDGF1_MOUSE) -
Teratocarcinoma-derived growth factor from Mus musculus
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Seq:
Struc:
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171 a.a.
40 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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J Med Chem
49:7054-7062
(2006)
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PubMed id:
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Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala.
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L.Calvanese,
A.Saporito,
D.Marasco,
G.D'Auria,
G.Minchiotti,
C.Pedone,
L.Paolillo,
L.Falcigno,
M.Ruvo.
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ABSTRACT
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We report here for the first time the solution structures at pH 3 and pH 6 of
the synthetic CFC domain of mouse Cripto and of the point mutated variant W107A
that is unable to bind to the Alk4 Cripto receptor. NMR data confirm that the
CFC domain has a C1-C4, C2-C6, C3-C5 disulfide pattern and show that structures
are rather flexible and globally extended, with three noncanonical antiparallel
strands. His104 and Trp107 side chains protrude from a protein edge and are
strongly exposed to solvent, supporting previous evidence of direct involvement
in receptor binding. On the opposite molecule side, several nonpolar residues
are gathered, forming a large hydrophobic patch that supposedly acts as
interface with the cell membrane or the adjacent EGF-like domain. A second
hydrophilic patch surrounding His104 and Trp107 is present only in the wild type
variant, suggesting a possible involvement in modulating Alk4 recognition.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Calvanese,
D.Marasco,
N.Doti,
A.Saporito,
G.D'Auria,
L.Paolillo,
M.Ruvo,
and
L.Falcigno
(2010).
Structural investigations on the Nodal-Cripto binding: a theoretical and experimental approach.
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Biopolymers,
93,
1011-1021.
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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.
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Links
