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.


1y93

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1y93.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1y93.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1y93| PDB=1y93 | SCENE= }}
{{STRUCTURE_1y93| PDB=1y93 | SCENE= }}
-
'''Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution'''
+
===Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution===
-
==Overview==
+
<!--
-
The structures of the catalytic domain of matrix metalloproteinase 12 in the presence of acetohydroxamic acid and N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid have been solved by x-ray diffraction in the crystalline state at 1.0 and 1.3-A resolution, respectively, and compared with the previously published x-ray structure at 1.2-A resolution of the adduct with batimastat. The structure of the N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid adduct has been solved by NMR in solution. The three x-ray structures and the solution structure are similar but not identical to one another, the differences being sizably higher in the loops. We propose that many of the loops show a dynamical behavior in solution on a variety of time scales. Different conformations of some flexible regions of the protein can be observed as "frozen" in different crystalline environments. The mobility in solution studied by NMR reveals conformational equilibria in accessible time scales, i.e., from 10(-5) s to ms and more. Averaging of some residual dipolar couplings is consistent with further motions down to 10(-9) s. Finally, local thermal motions of each frozen conformation in the crystalline state at 100 K correlate well with local motions on the picosecond time scale. Flexibility/conformational heterogeneity in crucial parts of the catalytic domain is a rule rather than an exception in matrix metalloproteinases, and its extent may be underestimated by inspection of one x-ray structure. Backbone flexibility may play a role in the difficulties encountered in the design of selective inhibitors, whereas it may be a requisite for substrate binding and broad substrate specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15809432}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15809432 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15809432}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Conformational variability of matrix metalloproteinases: beyond a single 3D structure., Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5334-9. Epub 2005 Apr 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15809432 15809432]
Conformational variability of matrix metalloproteinases: beyond a single 3D structure., Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5334-9. Epub 2005 Apr 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15809432 15809432]
 +
 +
X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases., Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B, Angew Chem Int Ed Engl. 2003 Jun 16;42(23):2673-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12813751 12813751]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Macrophage elastase]]
Line 37: Line 43:
[[Category: Metallo elastase]]
[[Category: Metallo elastase]]
[[Category: Mmp12]]
[[Category: Mmp12]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:01:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:22:13 2008''

Revision as of 16:22, 27 July 2008

Image:1y93.png

Template:STRUCTURE 1y93

Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution

Template:ABSTRACT PUBMED 15809432

About this Structure

1Y93 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational variability of matrix metalloproteinases: beyond a single 3D structure., Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5334-9. Epub 2005 Apr 4. PMID:15809432

X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases., Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B, Angew Chem Int Ed Engl. 2003 Jun 16;42(23):2673-6. PMID:12813751

Page seeded by OCA on Sun Jul 27 19:22:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y93"
Personal tools