PDBsum entry 1k0x

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protein links
Hormone/growth factor PDB id
Protein chain
108 a.a. *
* Residue conservation analysis
PDB id:
Name: Hormone/growth factor
Title: Solution structure of melanoma inhibitory activity protein
Structure: Melanoma derived growth regulatory protein. Chain: a. Synonym: melanoma inhibitory activity. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: J.C.Lougheed,P.J.Domaille,T.M.Handel
Key ref: J.C.Lougheed et al. (2002). Solution structure and dynamics of melanoma inhibitory activity protein. J Biomol NMR, 22, 211-223. PubMed id: 11991352
21-Sep-01     Release date:   24-Jul-02    
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Protein chain
Pfam   ArchSchema ?
Q16674  (MIA_HUMAN) -  Melanoma-derived growth regulatory protein
131 a.a.
108 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     cell proliferation   1 term 
  Biochemical function     growth factor activity     1 term  


J Biomol NMR 22:211-223 (2002)
PubMed id: 11991352  
Solution structure and dynamics of melanoma inhibitory activity protein.
J.C.Lougheed, P.J.Domaille, T.M.Handel.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20303980 M.Guttman, J.H.Prieto, T.M.Handel, P.J.Domaille, and E.A.Komives (2010).
Structure of the minimal interface between ApoE and LRP.
  J Mol Biol, 398, 306-319.
PDB codes: 2knx 2kny
15692736 M.Fossi, J.Linge, D.Labudde, D.Leitner, M.Nilges, and H.Oschkinat (2005).
Influence of chemical shift tolerances on NMR structure calculations using ARIA protocols for assigning NOE data.
  J Biomol NMR, 31, 21-34.  
12592021 R.Stoll, C.Renner, R.Buettner, W.Voelter, A.K.Bosserhoff, and T.A.Holak (2003).
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
  Protein Sci, 12, 510-519.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.