PMID- 10356396
OWN - NLM
STAT- MEDLINE
DCOM- 19990622
LR  - 20190619
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 284
IP  - 5420
DP  - 1999 Jun 4
TI  - Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
PG  - 1667-70
AB  - Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation.
      Control of their activity is a promising target for therapy of diseases
      characterized by abnormal connective tissue turnover. MMPs are expressed as
      latent proenzymes that are activated by proteolytic cleavage that triggers a
      conformational change in the propeptide (cysteine switch). The structure of
      proMMP-2 reveals how the propeptide shields the catalytic cleft and that the
      cysteine switch may operate through cleavage of loops essential for propeptide
      stability.
FAU - Morgunova, E
AU  - Morgunova E
AD  - Division of Matrix Biology, Department of Medical Biochemistry and Biophysics,
      Karolinska Institute, Stockholm, Sweden.
FAU - Tuuttila, A
AU  - Tuuttila A
FAU - Bergmann, U
AU  - Bergmann U
FAU - Isupov, M
AU  - Isupov M
FAU - Lindqvist, Y
AU  - Lindqvist Y
FAU - Schneider, G
AU  - Schneider G
FAU - Tryggvason, K
AU  - Tryggvason K
LA  - eng
SI  - PDB/1CK7
PT  - Comment
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Enzyme Precursors)
RN  - 0 (Fibronectins)
RN  - 9013-71-2 (Hemopexin)
RN  - EC 3.4.24.- (Gelatinases)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.24 (Matrix Metalloproteinase 2)
SB  - IM
CON - Science. 1999 Jun 4;284(5420):1600-1. PMID: 10383332
MH  - Amino Acid Sequence
MH  - Catalytic Domain
MH  - Enzyme Activation
MH  - Enzyme Precursors/*chemistry/metabolism
MH  - Fibronectins/chemistry
MH  - Gelatinases/*chemistry/metabolism
MH  - Hemopexin/chemistry
MH  - Humans
MH  - Hydrogen Bonding
MH  - Matrix Metalloproteinase 2
MH  - Metalloendopeptidases/*chemistry/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Protein Folding
MH  - Protein Structure, Secondary
EDAT- 1999/06/05 00:00
MHDA- 1999/06/05 00:01
CRDT- 1999/06/05 00:00
PHST- 1999/06/05 00:00 [pubmed]
PHST- 1999/06/05 00:01 [medline]
PHST- 1999/06/05 00:00 [entrez]
AID - 10.1126/science.284.5420.1667 [doi]
PST - ppublish
SO  - Science. 1999 Jun 4;284(5420):1667-70. doi: 10.1126/science.284.5420.1667.