Linked Life Data

15124932

Source:http://linkedlifedata.com/resource/pubmed/id/15124932

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-5-4
pubmed:abstractText
We report a molecular dynamics simulation study of a zinc-protease--gelatinase A or MMP2--which is a major target for drug design, being involved in tumor metastasis and other degenerative diseases. Two structures have been employed as starting conditions, one based on the crystal of multi-domain proMMP2, the other consisting of the catalytic domain only. The overall fold of the two models is maintained over the 1260 ps trajectory, enabling us to analyze correlations of fluctuations among domains, and to observe the presence of correlations within the catalytic domain in the multi-domain enzyme only, hence due to the presence of hemopexin and fibronectin domains. In the multi-domain protein, two cavities are conserved over the trajectory, one of them pointing to a key region, a crevice surrounding the catalytic zinc. The other one is localized across the three domains of the MMP2 metalloproteinase. These areas are partially covered by the propeptide in the crystal structure of proMMP2. We propose a model of MMP2-collagen interaction that involves both identified cavities and takes into account the inter/intra domain cross-correlations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0920-654X
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
837-48
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Molecular dynamics simulation of matrix metalloproteinase 2: fluctuations and time evolution of recognition pockets.
pubmed:affiliation
INFM and Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 1-00133 Rome, Italy.
pubmed:publicationType
Journal Article