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Covalent modification of matrix metalloproteinases by a photoaffinity probe: influence of nucleophilicity and flexibility of the residue in position 241.

Abstract:

A photoaffinity probe, developed for the specific labeling of matrix metalloproteinase (MMP) active sites, was recently shown to covalently modify a single residue in human MMP-12, namely, Lys(241), by reacting selectively with the side chain epsilon-amino group of that residue. The residue in position 241 of MMPs is not conserved; thus, variability in this position may be responsible for the dispersion in cross-linking yield observed between MMPs when labeled by this photoaffinity probe. By ...

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Publication status:
Published

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Publisher copy:
10.1021/bc800478b

Authors


Dabert-Gay, AS More by this author
Lajeunesse, E More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
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Journal:
Bioconjugate chemistry
Volume:
20
Issue:
2
Pages:
367-375
Publication date:
2009-02-05
DOI:
EISSN:
1520-4812
ISSN:
1043-1802
URN:
uuid:20356674-2c2a-4145-ace4-b1f259f339e3
Source identifiers:
226979
Local pid:
pubs:226979

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