1d2b: Difference between revisions

Revision as of 22:11, 30 June 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:1d2b.png

Template:STRUCTURE 1d2b

THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURESTHE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES

Template:ABSTRACT PUBMED 10623524

About this StructureAbout this Structure

1D2B is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases., Wu B, Arumugam S, Gao G, Lee GI, Semenchenko V, Huang W, Brew K, Van Doren SR, J Mol Biol. 2000 Jan 14;295(2):257-68. PMID:10623524

Page seeded by OCA on Mon Jun 30 22:11:17 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1d2b.jpg|left|200px]]
+{{Seed}}
+[[Image:1d2b.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1d2b|  PDB=1d2b  |  SCENE=  }}
-'''THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES'''
+===THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES===
-==Overview==
+<!--
-A high quality solution structure of the matrix metalloproteinase inhibitory N-terminal domain of recombinant human tissue inhibitor of metalloproteinases-1 (N-TIMP-1) has been determined. For the rigidly packed residues, the average RMSD to the mean structure is 0. 57 A for the backbone atoms and 1.00 A for all heavy atoms. Comparison of the solution structure of free N-TIMP-1 with the crystal structure of TIMP-1 bound to the catalytic domain of MMP-3 ( Gomis-R]uth et al., 1997 ) shows that the structural core of the beta barrel flanked by helices is nearly unchanged by the association with MMP-3, evident from a backbone RMSD of 1.15 A. However, clear differences in the conformation of the MMP-binding ridge of free and MMP-bound TIMP-1 suggest induced fit throughout the ridge. The MMP-dependent conformational changes in the ridge include a dramatic bending of AB loop residues Glu28 through Leu34, moderate hinge bending of the CD-loop about residues Ala65 and Cys70, and modest bending of the Cys1 through Pro6 segment. A large number of interresidue Nuclear Overhauser enhancements (NOEs) augmented by stereospecific assignments, torsion restraints, and dipolar couplings (an average of 18 non-trivial restraints per residue) engender confidence in these structural inferences. A tight cluster of three lysine residues and one arginine residue atop beta-strands A and B, and identical among TIMP sequences, form the heart of a highly conserved electropositive patch that may interact with anionic components of the extracellular matrix.
+The line below this paragraph, {{ABSTRACT_PUBMED_10623524}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10623524 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10623524}}
 ==About this Structure==
-D2B 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=1D2B OCA].
+D2B 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=1D2B OCA].
 ==Reference==
@@ Line 31: / Line 35: @@
 [[Category: Ob-fold]]
 [[Category: Protease inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:22:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:11:17 2008''