This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2jsd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2jsd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jsd" /> '''Solution structure of MMP20 complexed with N...)
Line 4: Line 4:
==Overview==
==Overview==
-
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.
+
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.
==About this Structure==
==About this Structure==
Line 17: Line 17:
[[Category: Bertini, I.]]
[[Category: Bertini, I.]]
[[Category: Cantini, F.]]
[[Category: Cantini, F.]]
-
[[Category: Conte, R.Del.]]
+
[[Category: Conte, R Del.]]
[[Category: Cozzi, R.]]
[[Category: Cozzi, R.]]
[[Category: Gonnelli, L.]]
[[Category: Gonnelli, L.]]
-
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
+
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: CA]]
[[Category: CA]]
[[Category: NGH]]
[[Category: NGH]]
Line 32: Line 32:
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:08:28 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:38 2008''

Revision as of 16:05, 21 February 2008


2jsd

Drag the structure with the mouse to rotate

Solution structure of MMP20 complexed with NNGH

Overview

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.

About this Structure

2JSD is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase., Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L, FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6. PMID:17869250

Page seeded by OCA on Thu Feb 21 18:05:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools