Linked Life Data

17869250

Source:http://linkedlifedata.com/resource/pubmed/id/17869250

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2007-9-24
pubmed:abstractText
The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
581
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4723-6
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
pubmed:affiliation
ProtEra S.r.l., Via delle Idee 22, 50019 Sesto Fiorentino (FI), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't