PMID- 10623524
OWN - NLM
STAT- MEDLINE
DCOM- 20000215
LR  - 20071114
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 295
IP  - 2
DP  - 2000 Jan 14
TI  - NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized
      induced fit in recognition of matrix metalloproteinases.
PG  - 257-68
AB  - A high quality solution structure of the matrix metalloproteinase inhibitory
      N-terminal domain of recombinant human tissue inhibitor of metalloproteinases-1
      (N-TIMP-1) has been determined. For the rigidly packed residues, the average RMSD
      to the mean structure is 0. 57 A for the backbone atoms and 1.00 A for all heavy 
      atoms. Comparison of the solution structure of free N-TIMP-1 with the crystal
      structure of TIMP-1 bound to the catalytic domain of MMP-3 ( Gomis-R]uth et al., 
      1997 ) shows that the structural core of the beta barrel flanked by helices is
      nearly unchanged by the association with MMP-3, evident from a backbone RMSD of
      1.15 A. However, clear differences in the conformation of the MMP-binding ridge
      of free and MMP-bound TIMP-1 suggest induced fit throughout the ridge. The
      MMP-dependent conformational changes in the ridge include a dramatic bending of
      AB loop residues Glu28 through Leu34, moderate hinge bending of the CD-loop about
      residues Ala65 and Cys70, and modest bending of the Cys1 through Pro6 segment. A 
      large number of interresidue Nuclear Overhauser enhancements (NOEs) augmented by 
      stereospecific assignments, torsion restraints, and dipolar couplings (an average
      of 18 non-trivial restraints per residue) engender confidence in these structural
      inferences. A tight cluster of three lysine residues and one arginine residue
      atop beta-strands A and B, and identical among TIMP sequences, form the heart of 
      a highly conserved electropositive patch that may interact with anionic
      components of the extracellular matrix.
CI  - Copyright 2000 Academic Press.
FAU - Wu, B
AU  - Wu B
AD  - Department of Biochemistry, University of Missouri, 117 Schweitzer Hall,
      Columbia, MO 65211, USA.
FAU - Arumugam, S
AU  - Arumugam S
FAU - Gao, G
AU  - Gao G
FAU - Lee, G I
AU  - Lee GI
FAU - Semenchenko, V
AU  - Semenchenko V
FAU - Huang, W
AU  - Huang W
FAU - Brew, K
AU  - Brew K
FAU - Van Doren, S R
AU  - Van Doren SR
LA  - eng
SI  - PDB/1D2B
GR  - AR40994/AR/NIAMS NIH HHS/United States
GR  - GM57289/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tissue Inhibitor of Metalloproteinase-1)
RN  - EC 3.4.24.- (Matrix Metalloproteinases)
SB  - IM
MH  - Catalytic Domain
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Matrix Metalloproteinases/*metabolism
MH  - Models, Molecular
MH  - Protein Conformation
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Surface Properties
MH  - Tissue Inhibitor of Metalloproteinase-1/*chemistry/metabolism
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.1999.3362 [doi]
AID - S0022-2836(99)93362-4 [pii]
PST - ppublish
SO  - J Mol Biol. 2000 Jan 14;295(2):257-68. doi: 10.1006/jmbi.1999.3362.