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2tmp
From Proteopedia
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N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP-2), NMR, 49 STRUCTURES
Overview
The high resolution structure of the N-terminal domain of tissue inhibitor, of metalloproteinases-2 (N-TIMP-2) in solution has been determined using, multidimensional heteronuclear NMR spectroscopy, with the structural, calculations based on an extensive set of constraints, including 3132, nuclear Overhauser effect-based distance constraints, 56 hydrogen bond, constraints, and 220 torsion angle constraints (an average of 26.9, constraints/residue). The core of the protein consists of a five-stranded, beta-barrel that is homologous to the beta-barrel found in the, oligosaccharide/oligonucleotide binding protein fold. The binding site for, the catalytic domain of matrix metalloproteinases-3 (N-MMP-3) on N-TIMP-2, has been mapped by determining the changes in chemical shifts on complex, formation for signals from the protein backbone (15N, 13C, and 1H). This, approach identified a discrete N-MMP-3 binding site on N-TIMP-2 composed, of the N terminus of the protein and the loops between beta-strands AB, CD, and EF. The beta-hairpin formed from strands A and B in N-TIMP-2 is, significantly longer than the equivalent structure in TIMP-1, allowing it, to make more extensive binding interactions with the MMP catalytic domain., A detailed comparison of the N-TIMP-2 structure with that of TIMP-1 bound, to N-MMP-3 (Gomis-Ruth, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H. , Brew, K., Bourne, G. P., Bartunik, H. & Bode, W. (1997) Nature 389, 77-80) revealed that the core, beta-barrels are very similar in topology but that the loop connecting, beta-strands CD (P67-C72) would need to undergo a large conformational, change for TIMP-2 to bind in a similar manner to TIMP-1.
About this Structure
2TMP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3., Muskett FW, Frenkiel TA, Feeney J, Freedman RB, Carr MD, Williamson RA, J Biol Chem. 1998 Aug 21;273(34):21736-43. PMID:9705310
Page seeded by OCA on Mon Nov 12 23:38:31 2007
