Publication Date:
1999-06-05
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morgunova, E -- Tuuttila, A -- Bergmann, U -- Isupov, M -- Lindqvist, Y -- Schneider, G -- Tryggvason, K -- New York, N.Y. -- Science. 1999 Jun 4;284(5420):1667-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10356396" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Catalytic Domain
;
Enzyme Activation
;
Enzyme Precursors/*chemistry/metabolism
;
Fibronectins/chemistry
;
Gelatinases/*chemistry/metabolism
;
Hemopexin/chemistry
;
Humans
;
Hydrogen Bonding
;
Matrix Metalloproteinase 2
;
Metalloendopeptidases/*chemistry/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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