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PDBsum entry 1uaw

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protein links
RNA binding protein PDB id
1uaw
Jmol
Contents
Protein chain
77 a.a. *
* Residue conservation analysis
PDB id:
1uaw
Name: RNA binding protein
Title: Solution structure of the n-terminal RNA-binding domain of mouse musashi1
Structure: Mouse-musashi-1. Chain: a. Fragment: n-terminal RNA-binding domain. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Tissue: neural stem. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 15 models
Authors: Y.Miyanoiri,H.Kobayashi,M.Watanabe,T.Ikeda,T.Nagata,H.Okano, S.Uesugi,M.Katahira
Key ref:
Y.Miyanoiri et al. (2003). Origin of higher affinity to RNA of the N-terminal RNA-binding domain than that of the C-terminal one of a mouse neural protein, musashi1, as revealed by comparison of their structures, modes of interaction, surface electrostatic potentials, and backbone dynamics. J Biol Chem, 278, 41309-41315. PubMed id: 12907678 DOI: 10.1074/jbc.M306210200
Date:
24-Mar-03     Release date:   24-Mar-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q61474  (MSI1H_MOUSE) -  RNA-binding protein Musashi homolog 1
Seq:
Struc:
362 a.a.
77 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleotide binding     2 terms  

 

 
DOI no: 10.1074/jbc.M306210200 J Biol Chem 278:41309-41315 (2003)
PubMed id: 12907678  
 
 
Origin of higher affinity to RNA of the N-terminal RNA-binding domain than that of the C-terminal one of a mouse neural protein, musashi1, as revealed by comparison of their structures, modes of interaction, surface electrostatic potentials, and backbone dynamics.
Y.Miyanoiri, H.Kobayashi, T.Imai, M.Watanabe, T.Nagata, S.Uesugi, H.Okano, M.Katahira.
 
  ABSTRACT  
 
Musashi1 is an RNA-binding protein abundantly expressed in the developing mouse central nervous system. Its restricted expression in neural precursor cells suggests that it is involved in maintenance of the character of progenitor cells. Musashi1 contains two ribonucleoprotein-type RNA-binding domains (RBDs), RBD1 and RBD2, the affinity to RNA of RBD1 being much higher than that of RBD2. We previously reported the structure and mode of interaction with RNA of RBD2. Here, we have determined the structure and mode of interaction with RNA of RBD1. We have also analyzed the surface electrostatic potential and backbone dynamics of both RBDs. The two RBDs exhibit the same ribo-nucleoprotein-type fold and commonly make contact with RNA on the beta-sheet side. On the other hand, there is a remarkable difference in surface electrostatic potential, the beta-sheet of RBD1 being positively charged, which is favorable for binding negatively charged RNA, but that of RBD2 being almost neutral. There is also a difference in backbone dynamics, the central portion of the beta-sheet of RBD1 being flexible, but that of RBD2 not being flexible. The flexibility of RBD1 may be utilized in the recognition process to facilitate an induced fit. Thus, comparative studies have revealed the origin of the higher affinity of RBD1 than that of RBD2 and indicated that the affinity of an RBD to RNA is not governed by its fold alone but is also determined by its surface electrostatic potential and/or backbone dynamics. The biological role of RBD2 with lower affinity is also discussed.
 
  Selected figure(s)  
 
Figure 1.
FIG. 1. Gel retardation experiments as to RBD1, RBD2, and RBD1-RBD2. As shown in A, 4 fmol of 32P-labeled r(GUUAGUUAGUUAGUU) (T4-3) was incubated with 0, 1.5, 4.4, 13, 40, and 120 pmol of either RBD1 (lanes 1-6) or RBD2 (lanes 7-12). The mixtures were run on polyacrylamide gel. As shown in B, 4 fmol of 32P-labeled T4-3 was incubated with 0, 0.008, 0.04, 0.2, 1, and 5 pmol of RBD1-RBD2 and run on polyacrylamide gel (lanes 1-6).
Figure 5.
FIG. 5. The surface electrostatic potential. A, Musashi1 RBD1; B, RBD2. Positive surface potential > +5K[B]T and negative surface potential < -5K[B]T are represented in blue and red, respectively, where K[B] is the Boltzmann constant and T is the absolute temperature.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 41309-41315) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19153609 A.Furukawa, T.Nagata, A.Matsugami, Y.Habu, R.Sugiyama, F.Hayashi, N.Kobayashi, S.Yokoyama, H.Takaku, and M.Katahira (2009).
Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G.
  EMBO J, 28, 440-451.
PDB code: 2kbo
18419830 F.Ye, C.Zhou, Q.Cheng, J.Shen, and H.Chen (2008).
Stem-cell-abundant proteins Nanog, Nucleostemin and Musashi1 are highly expressed in malignant cervical epithelial cells.
  BMC Cancer, 8, 108.  
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 code is shown on the right.