PMID- 10623522
OWN - NLM
STAT- MEDLINE
DCOM- 20000215
LR  - 20171116
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 295
IP  - 2
DP  - 2000 Jan 14
TI  - Solution structure and backbone dynamics of the second PDZ domain of postsynaptic
      density-95.
PG  - 225-37
AB  - The second PDZ domain of postsynaptic density-95 (PSD-95 PDZ2) plays a critical
      role in coupling N-methyl-D-aspartate receptors to neuronal nitric oxide synthase
      (nNOS). In this work, the solution structure of PSD-95 PDZ2 was determined to
      high resolution by NMR spectroscopy. The structure of PSD-95 PDZ2 was compared in
      detail with that of alpha1-syntrophin PDZ domain, as the PDZ domains share
      similar target interaction properties. The interaction of the PSD-95 PDZ2 with a 
      carboxyl-terminal peptide derived from a cytoplasmic protein CAPON was studied by
      NMR titration experiments. Complex formation between PSD-95 PDZ2 and the nNOS PDZ
      was modelled on the basis of the crystal structure of the alpha1-syntrophin
      PDZ/nNOS PDZ dimer. We found that the prolonged loop connecting the betaB and
      betaC strands of PSD-95 PDZ2 is likely to play a role in both the binding of the 
      carboxyl-terminal peptide and the nNOS beta-finger. Finally, the backbone
      dynamics of the PSD-95 PDZ2 in the absence of bound peptide were studied using a 
      model-free approach. The "GLGF"-loop and the loop connecting alphaB and betaF of 
      the protein display some degree of flexibility in solution. The rest of the
      protein is rigid and lacks detectable slow time-scale (microseconds to
      milliseconds) motions. In particular, the loop connecting betaB and betaC loop
      adopts a well-defined, rigid structure in solution. It appears that the loop
      adopts a pre-aligned conformation for the PDZ domain to interact with its
      targets.
CI  - Copyright 2000 Academic Press.
FAU - Tochio, H
AU  - Tochio H
AD  - Department of Biochemistry, The Hong Kong University of Science and Technology,
      Clear Water Bay, Hong Kong, Kowloon, P. R. China.
FAU - Hung, F
AU  - Hung F
FAU - Li, M
AU  - Li M
FAU - Bredt, D S
AU  - Bredt DS
FAU - Zhang, M
AU  - Zhang M
LA  - eng
SI  - PDB/1QLC
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (DNA Primers)
RN  - 0 (Disks Large Homolog 4 Protein)
RN  - 0 (Dlg4 protein, rat)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Solutions)
RN  - 0 (postsynaptic density proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - DNA Primers
MH  - Disks Large Homolog 4 Protein
MH  - Intracellular Signaling Peptides and Proteins
MH  - Magnetic Resonance Spectroscopy
MH  - Membrane Proteins
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*chemistry/genetics/isolation & purification
MH  - Protein Conformation
MH  - Rats
MH  - Recombinant Proteins/chemistry/genetics/isolation & purification
MH  - Sequence Homology, Amino Acid
MH  - Solutions
EDAT- 2000/01/07 09:00
MHDA- 2000/02/19 09:00
CRDT- 2000/01/07 09:00
PHST- 2000/01/07 09:00 [pubmed]
PHST- 2000/02/19 09:00 [medline]
PHST- 2000/01/07 09:00 [entrez]
AID - 10.1006/jmbi.1999.3350 [doi]
AID - S0022-2836(99)93350-8 [pii]
PST - ppublish
SO  - J Mol Biol. 2000 Jan 14;295(2):225-37. doi: 10.1006/jmbi.1999.3350.