1cxw: Difference between revisions

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[[Image:1cxw.gif|left|200px]]<br />

[[Image:1cxw.gif|left|200px]]<br /><applet load="1cxw" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1cxw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1cxw" />

'''THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2'''<br />

==Overview==

BACKGROUND: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type, IV collagenase) has an important role in extracellular matrix degradation, during cell migration and tissue remodeling. It is involved in, development, inflammation, wound healing, tumor invasion, metastasis and, other physiological and pathological processes. The enzyme cleaves several, types of collagen, elastin, fibronectin and laminin. Binding to collagen, is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active, site. RESULTS: We have determined the NMR solution structure of the second, type II module from human MMP-2 (col-2). The module exhibits a typical, type II fold with two short double-stranded antiparallel beta sheets and, three large loops packed around a cluster of conserved aromatic residues., Backbone amide dynamics, derived from (15)N relaxation experiments, correlate well with solvent accessibility and intramolecular hydrogen, bonding. A synthetic peptide with the collagen consensus sequence, (Pro-Pro-Gly)(6), is shown to interact with the module. CONCLUSIONS:, Spectral perturbations induced by (Pro-Pro-Gly)(6) binding reveal the, region involved in the interaction of col-2 with collagen. The binding, surface comprises exposed aromatic residues Phe21, Tyr38, Trp40, Tyr47, Tyr53 and Phe55, and the neighboring Gly33-Gly37 segment.

BACKGROUND: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type IV collagenase) has an important role in extracellular matrix degradation during cell migration and tissue remodeling. It is involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes. The enzyme cleaves several types of collagen, elastin, fibronectin and laminin. Binding to collagen is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active site. RESULTS: We have determined the NMR solution structure of the second type II module from human MMP-2 (col-2). The module exhibits a typical type II fold with two short double-stranded antiparallel beta sheets and three large loops packed around a cluster of conserved aromatic residues. Backbone amide dynamics, derived from (15)N relaxation experiments, correlate well with solvent accessibility and intramolecular hydrogen bonding. A synthetic peptide with the collagen consensus sequence, (Pro-Pro-Gly)(6), is shown to interact with the module. CONCLUSIONS: Spectral perturbations induced by (Pro-Pro-Gly)(6) binding reveal the region involved in the interaction of col-2 with collagen. The binding surface comprises exposed aromatic residues Phe21, Tyr38, Trp40, Tyr47, Tyr53 and Phe55, and the neighboring Gly33-Gly37 segment.

==Disease==

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==About this Structure==

1CXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CXW OCA].

1CXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXW OCA].

==Reference==

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[[Category: beta sheet]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:26:~~33 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:50 2008''

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-[[Image:1cxw.gif|left|200px]]<br />
+[[Image:1cxw.gif|left|200px]]<br /><applet load="1cxw" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1cxw" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1cxw" />
 '''THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2'''<br />
 ==Overview==
-BACKGROUND: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type, IV collagenase) has an important role in extracellular matrix degradation, during cell migration and tissue remodeling. It is involved in, development, inflammation, wound healing, tumor invasion, metastasis and, other physiological and pathological processes. The enzyme cleaves several, types of collagen, elastin, fibronectin and laminin. Binding to collagen, is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active, site. RESULTS: We have determined the NMR solution structure of the second, type II module from human MMP-2 (col-2). The module exhibits a typical, type II fold with two short double-stranded antiparallel beta sheets and, three large loops packed around a cluster of conserved aromatic residues., Backbone amide dynamics, derived from (15)N relaxation experiments, correlate well with solvent accessibility and intramolecular hydrogen, bonding. A synthetic peptide with the collagen consensus sequence, (Pro-Pro-Gly)(6), is shown to interact with the module. CONCLUSIONS:, Spectral perturbations induced by (Pro-Pro-Gly)(6) binding reveal the, region involved in the interaction of col-2 with collagen. The binding, surface comprises exposed aromatic residues Phe21, Tyr38, Trp40, Tyr47, Tyr53 and Phe55, and the neighboring Gly33-Gly37 segment.
+BACKGROUND: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type IV collagenase) has an important role in extracellular matrix degradation during cell migration and tissue remodeling. It is involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes. The enzyme cleaves several types of collagen, elastin, fibronectin and laminin. Binding to collagen is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active site. RESULTS: We have determined the NMR solution structure of the second type II module from human MMP-2 (col-2). The module exhibits a typical type II fold with two short double-stranded antiparallel beta sheets and three large loops packed around a cluster of conserved aromatic residues. Backbone amide dynamics, derived from (15)N relaxation experiments, correlate well with solvent accessibility and intramolecular hydrogen bonding. A synthetic peptide with the collagen consensus sequence, (Pro-Pro-Gly)(6), is shown to interact with the module. CONCLUSIONS: Spectral perturbations induced by (Pro-Pro-Gly)(6) binding reveal the region involved in the interaction of col-2 with collagen. The binding surface comprises exposed aromatic residues Phe21, Tyr38, Trp40, Tyr47, Tyr53 and Phe55, and the neighboring Gly33-Gly37 segment.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-CXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CXW OCA].
+CXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXW OCA].
 ==Reference==
@@ Line 27: / Line 26: @@
 [[Category: beta sheet]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:26:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:50 2008''