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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I.Bertini,
M.Fragai,
C.Luchinat,
M.Melikian,
and
C.Venturi
(2009).
Characterisation of the MMP-12-elastin adduct.
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Chemistry, 15,
7842-7845.
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H.Kobayashi,
N.Morisaki,
H.Miyachi,
and
Y.Hashimoto
(2008).
Coordination of divalent metal cation to amide group to form adduct ion in FAB mass spectrometry: implication of Zn2+ in enzymatic hydrolysis of amide bond.
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Chem Pharm Bull (Tokyo), 56,
672-676.
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L.A.Alcaraz,
L.Banci,
I.Bertini,
F.Cantini,
A.Donaire,
and
L.Gonnelli
(2007).
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.
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J Biol Inorg Chem, 12,
1197-1206.
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PDB codes:
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D.E.Danley
(2006).
Crystallization to obtain protein-ligand complexes for structure-aided drug design.
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Acta Crystallogr D Biol Crystallogr, 62,
569-575.
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I.Bertini,
V.Calderone,
M.Fragai,
C.Luchinat,
M.Maletta,
and
K.J.Yeo
(2006).
Snapshots of the reaction mechanism of matrix metalloproteinases.
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Angew Chem Int Ed Engl, 45,
7952-7955.
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PDB codes:
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S.Iyer,
R.Visse,
H.Nagase,
and
K.R.Acharya
(2006).
Crystal structure of an active form of human MMP-1.
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J Mol Biol, 362,
78-88.
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PDB code:
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G.Grasso,
R.D'Agata,
E.Rizzarelli,
G.Spoto,
L.D'Andrea,
C.Pedone,
A.Picardi,
A.Romanelli,
M.Fragai,
and
K.J.Yeo
(2005).
Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au (111) surfaces monitored by ESI-MS.
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J Mass Spectrom, 40,
1565-1571.
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P.L.Tsai,
C.H.Chen,
C.J.Huang,
C.M.Chou,
and
G.D.Chang
(2004).
Purification and cloning of an endogenous protein inhibitor of carp nephrosin, an astacin metalloproteinase.
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J Biol Chem, 279,
11146-11155.
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L.Watanabe,
J.D.Shannon,
R.H.Valente,
A.Rucavado,
A.Alape-Girón,
A.S.Kamiguti,
R.D.Theakston,
J.W.Fox,
J.M.Gutiérrez,
and
R.K.Arni
(2003).
Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.
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Protein Sci, 12,
2273-2281.
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PDB code:
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A.G.Pavlovsky,
M.G.Williams,
Q.Z.Ye,
D.F.Ortwine,
C.F.Purchase,
A.D.White,
V.Dhanaraj,
B.D.Roth,
L.L.Johnson,
D.Hupe,
C.Humblet,
and
T.L.Blundell
(1999).
X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.
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Protein Sci, 8,
1455-1462.
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PDB codes:
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F.J.Moy,
P.K.Chanda,
J.M.Chen,
S.Cosmi,
W.Edris,
J.S.Skotnicki,
J.Wilhelm,
and
R.Powers
(1999).
NMR solution structure of the catalytic fragment of human fibroblast collagenase complexed with a sulfonamide derivative of a hydroxamic acid compound.
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Biochemistry, 38,
7085-7096.
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PDB code:
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G.N.Smith,
E.A.Mickler,
K.A.Hasty,
and
K.D.Brandt
(1999).
Specificity of inhibition of matrix metalloproteinase activity by doxycycline: relationship to structure of the enzyme.
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Arthritis Rheum, 42,
1140-1146.
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W.Bode,
C.Fernandez-Catalan,
F.Grams,
F.X.Gomis-Rüth,
H.Nagase,
H.Tschesche,
and
K.Maskos
(1999).
Insights into MMP-TIMP interactions.
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Ann N Y Acad Sci, 878,
73-91.
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A.Mucha,
P.Cuniasse,
R.Kannan,
F.Beau,
A.Yiotakis,
P.Basset,
and
V.Dive
(1998).
Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions.
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J Biol Chem, 273,
2763-2768.
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B.C.Finzel,
E.T.Baldwin,
G.L.Bryant,
G.F.Hess,
J.W.Wilks,
C.M.Trepod,
J.E.Mott,
V.P.Marshall,
G.L.Petzold,
R.A.Poorman,
T.J.O'Sullivan,
H.J.Schostarez,
and
M.A.Mitchell
(1998).
Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.
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Protein Sci, 7,
2118-2126.
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PDB code:
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B.P.Mari,
I.C.Anderson,
S.E.Mari,
Y.Ning,
Y.Lutz,
L.Kobzik,
and
M.A.Shipp
(1998).
Stromelysin-3 is induced in tumor/stroma cocultures and inactivated via a tumor-specific and basic fibroblast growth factor-dependent mechanism.
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J Biol Chem, 273,
618-626.
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F.J.Moy,
P.K.Chanda,
S.Cosmi,
M.R.Pisano,
C.Urbano,
J.Wilhelm,
and
R.Powers
(1998).
High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
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Biochemistry, 37,
1495-1504.
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PDB codes:
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I.L.Alberts,
K.Nadassy,
and
S.J.Wodak
(1998).
Analysis of zinc binding sites in protein crystal structures.
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Protein Sci, 7,
1700-1716.
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Y.H.Ding,
K.Javaherian,
K.M.Lo,
R.Chopra,
T.Boehm,
J.Lanciotti,
B.A.Harris,
Y.Li,
R.Shapiro,
E.Hohenester,
R.Timpl,
J.Folkman,
and
D.C.Wiley
(1998).
Zinc-dependent dimers observed in crystals of human endostatin.
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Proc Natl Acad Sci U S A, 95,
10443-10448.
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PDB code:
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M.Betz,
P.Huxley,
S.J.Davies,
Y.Mushtaq,
M.Pieper,
H.Tschesche,
W.Bode,
and
F.X.Gomis-Rüth
(1997).
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.
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Eur J Biochem, 247,
356-363.
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PDB code:
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Y.Zhang,
W.L.Dean,
and
R.D.Gray
(1997).
Cooperative binding of Ca2+ to human interstitial collagenase assessed by circular dichroism, fluorescence, and catalytic activity.
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J Biol Chem, 272,
1444-1447.
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C.H.Bu,
and
T.Pourmotabbed
(1996).
Mechanism of Ca2+-dependent activity of human neutrophil gelatinase B.
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J Biol Chem, 271,
14308-14315.
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H.Nagase,
and
G.B.Fields
(1996).
Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.
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Biopolymers, 40,
399-416.
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L.Bányai,
H.Tordai,
and
L.Patthty
(1996).
Structure and domain-domain interactions of the gelatin binding site of human 72-kilodalton type IV collagenase (gelatinase A, matrix metalloproteinase 2).
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J Biol Chem, 271,
12003-12008.
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Q.A.Sang,
and
D.A.Douglas
(1996).
Computational sequence analysis of matrix metalloproteinases.
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J Protein Chem, 15,
137-160.
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Y.Zhang,
and
R.D.Gray
(1996).
Characterization of folded, intermediate, and unfolded states of recombinant human interstitial collagenase.
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J Biol Chem, 271,
8015-8021.
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A.Beaumont,
M.J.O'Donohue,
N.Paredes,
N.Rousselet,
M.Assicot,
C.Bohuon,
M.C.Fournié-Zaluski,
and
B.P.Roques
(1995).
The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study.
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J Biol Chem, 270,
16803-16808.
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C.H.Bu,
and
T.Pourmotabbed
(1995).
Mechanism of activation of human neutrophil gelatinase B. Discriminating between the role of Ca2+ in activation and catalysis.
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J Biol Chem, 270,
18563-18569.
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J.W.Becker,
A.I.Marcy,
L.L.Rokosz,
M.G.Axel,
J.J.Burbaum,
P.M.Fitzgerald,
P.M.Cameron,
C.K.Esser,
W.K.Hagmann,
and
J.D.Hermes
(1995).
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
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Protein Sci, 4,
1966-1976.
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PDB codes:
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S.R.Van Doren,
A.V.Kurochkin,
W.Hu,
Q.Z.Ye,
L.L.Johnson,
D.J.Hupe,
and
E.R.Zuiderweg
(1995).
Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.
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Protein Sci, 4,
2487-2498.
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PDB codes:
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T.Pourmotabbed,
J.A.Aelion,
D.Tyrrell,
K.A.Hasty,
C.H.Bu,
and
C.L.Mainardi
(1995).
Role of the conserved histidine and aspartic acid residues in activity and stabilization of human gelatinase B: an example of matrix metalloproteinases.
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J Protein Chem, 14,
527-535.
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W.Stöcker,
F.Grams,
U.Baumann,
P.Reinemer,
F.X.Gomis-Rüth,
D.B.McKay,
and
W.Bode
(1995).
The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.
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Protein Sci, 4,
823-840.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
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shown on the right.
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162 a.a.
_CA
_ZN
