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PDBsum entry 1k0x
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Hormone/growth factor
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PDB id
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1k0x
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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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Solution structure and dynamics of melanoma inhibitory activity protein.
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Authors
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J.C.Lougheed,
P.J.Domaille,
T.M.Handel.
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Ref.
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J Biomol Nmr, 2002,
22,
211-223.
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PubMed id
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Abstract
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Melanoma inhibitory activity (MIA) is a small secreted protein that is
implicated in cartilage cell maintenance and melanoma metastasis. It is
representative of a recently discovered family of proteins that contain a Src
Homologous 3 (SH3) subdomain. While SH3 domains are normally found in
intracellular proteins and mediate protein-protein interactions via recognition
of polyproline helices, MIA is single-domain extracellular protein, and it
probably binds to a different class of ligands. Here we report the assignments,
solution structure, and dynamics of human MIA determined by heteronuclear NMR
methods. The structures were calculated in a semi-automated manner without
manual assignment of NOE crosspeaks, and have a backbone rmsd of 0.38 A over the
ordered regions of the protein. The structure consists of an SH3-like subdomain
with N- and C-terminal extensions of approximately 20 amino acids each that
together form a novel fold. The rmsd between the solution structure and our
recently reported crystal structure is 0.86 A over the ordered regions of the
backbone, and the main differences are localized to the most dynamic regions of
the protein. The similarity between the NMR and crystal structures supports the
use of automated NOE assignments and ambiguous restraints to accelerate the
calculation of NMR structures.
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