1oo9: Difference between revisions
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'''Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings'''<br /> | '''Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OO9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] Full crystallographic information is available from [http:// | 1OO9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:34:42 2008'' | ||
Revision as of 17:34, 15 February 2008
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Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings
OverviewOverview
Crystal structures of catalytic domains of MMP-3 and MT1-MMP bound to, TIMP-1 or TIMP-2, respectively, differ in the orientation of the TIMP in, the MMP active site. The orientation in solution of N-TIMP-1 in the MMP-3, active site has been investigated using residual dipolar couplings (RDCs)., Fitting of the RDCs to the X-ray structures of the complexes suggests, general agreement with the orientation of crystalline MMP-3(DeltaC) and, TIMP-1 and a large disparity from the orientation of crystalline, MT1-MMP(DeltaC) and TIMP-2. Rigid body docking of MMP-3 and N-TIMP-1 X-ray, coordinates using RDCs and intermolecular NOEs provided a time-averaged, orientation in solution differing from the crystal structure by a 5, degrees rotation toward the MT1-MMP(DeltaC)/TIMP-2 orientation. The slight, discrepancy in orientations in solution and crystal lies within the, experimental uncertainties. Intermolecular NOEs used in the docking, corroborated the accuracy of mapping the interface by a paramagnetic NMR, footprinting assay, a potential alternative source of contacts for, docking. Some uncertainty in the N-TIMP-1 orientation in the MMP-3 active, site, coupled with microsecond to millisecond fluctuations of the, MMP-binding ridge of N-TIMP-1 in the complex and flexibility in, MMP-3(DeltaC) S(1)' to S(3)' subsites, leaves open the possibility that, N-TIMP-1 might dynamically pivot a few degrees or more in the arc toward, the MT1-MMP(DeltaC)/TIMP-2 orientation. Differing TIMP orientations in MMP, active sites are more likely to result from structural differences in TIMP, AB hairpin loops than from crystal packing artifacts.
DiseaseDisease
Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250], Sorsby fundus dystrophy OMIM:[188826]
About this StructureAbout this Structure
1OO9 is a Protein complex structure of sequences from Homo sapiens. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.
ReferenceReference
Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings., Arumugam S, Van Doren SR, Biochemistry. 2003 Jul 8;42(26):7950-8. PMID:12834347
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