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PDBsum entry 2jt5
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Solution structure of matrix metalloproteinase 3 (mmp-3) in the presence of n-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid (mlc88)
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Structure:
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Stromelysin-1. Chain: a. Fragment: sequence database residues 105-265. Synonym: matrix metalloproteinase-3, mmp-3, transin-1, sl-1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp3, stmy1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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NMR struc:
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1 models
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Authors:
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L.A.Alcaraz,L.Banci,I.Bertini,F.Cantini,A.Donaire,L.Gonnelli
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Key ref:
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L.A.Alcaraz
et al.
(2007).
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.
J Biol Inorg Chem,
12,
1197-1206.
PubMed id:
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Date:
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20-Jul-07
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Release date:
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19-Feb-08
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PROCHECK
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Headers
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References
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P08254
(MMP3_HUMAN) -
Stromelysin-1 from Homo sapiens
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Seq:
Struc:
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477 a.a.
161 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.4.24.17
- stromelysin 1.
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Reaction:
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Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
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Cofactor:
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Ca(2+); Zn(2+)
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J Biol Inorg Chem
12:1197-1206
(2007)
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PubMed id:
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Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.
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L.A.Alcaraz,
L.Banci,
I.Bertini,
F.Cantini,
A.Donaire,
L.Gonnelli.
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ABSTRACT
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We structurally characterized the adducts of the catalytic domain of matrix
metalloproteinase-3 (MMP3) with three different nonpeptidic inhibitors by
solving the solution structure of one adduct
[MMP3-N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid] and then by
calculating structural models of the other two adducts using a reduced set of
experimental NMR data, following a recently proposed procedure (Bertini et al.
in J. Med. Chem. 48:7544-7559, 2005). The inhibitors were selected with the
criteria of maintaining in all of them the same zinc-coordinating moiety and of
selectively changing the substituents and/or the functional groups. The backbone
dynamics on various time scales have been characterized as well. The comparison
among these structures and with others previously reported allowed us to
elucidate fine details of inhibitor-receptor interactions and to develop some
criteria, which could guide in optimizing the design of selective inhibitors.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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F.E.Jacobsen,
M.W.Buczynski,
E.A.Dennis,
and
S.M.Cohen
(2008).
A macrophage cell model for selective metalloproteinase inhibitor design.
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Chembiochem,
9,
2087-2095.
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M.J.Werle
(2008).
Cell-to-cell signaling at the neuromuscular junction: the dynamic role of the extracellular matrix.
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Ann N Y Acad Sci,
1132,
13-18.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
