1ks0: Difference between revisions

Revision as of 10:52, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ks0.png

Template:STRUCTURE 1ks0

The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2

Template:ABSTRACT PUBMED 11928808

About this StructureAbout this Structure

1KS0 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains., Gehrmann M, Briknarova K, Banyai L, Patthy L, Llinas M, Biol Chem. 2002 Jan;383(1):137-48. PMID:11928808

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2'''
+===The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2===
-==Overview==
+<!--
-Human matrix metalloproteinase-2 (MMP-2) contains three in-tandem fibronectin type II (FII) repeats that bind gelatin. Here, we report the NMR solution structure of the first FII module of MMP-2 (col-1). The latter is described as a characteristic, globular FII fold containing two beta-sheets, a stretch of 3(1)-helix, a turn of alpha-helix, and an exposed hydrophobic surface lined with aromatic residues. We show that col-1 binds (Pro-Pro-Gly)6, a mimic of gelatin, with a Ka of approx. 0.42 mm(-1), and that its binding site involves a number of aromatic residues as well as Arg34, as previously found for the second and third homologous repeats. Moreover, the affinity of the in-tandem col-1+2 construct (col-12) toward the longer ligand (Pro-Pro-Gly)12 is twice that for (Pro-Pro-Gly)6, as expected from mass action. A detailed structural comparison between FII and kringle domains indicates that four main conformational features are shared: two antiparallel beta-sheets, a central 3(1)-helix, and the quasiperpendicular orientation of the two proximal Cys-Cys bonds. Structure superposition by optimizing overlap of cystine bridge areas results in close juxtaposition of their main beta-sheets and 31-helices, and reveals that the gelatin binding site of FII modules falls at similar locations and exhibits almost identical topological features to those of the lysine binding site of kringle domains. Thus, despite the minor (&lt;15%) consensus sequence relating FII modules to kringles, there is a strong folding and binding site structural homology between the two domains, enforced by key common conformational determinants.
+The line below this paragraph, {{ABSTRACT_PUBMED_11928808}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11928808 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11928808}}
 ==About this Structure==
-KS0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KS0 OCA].
+KS0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KS0 OCA].
 ==Reference==
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 [[Category: Alpha helix]]
 [[Category: Beta sheet]]
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