Sandbox Reserved 478: Difference between revisions
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{{STRUCTURE_2clt| PDB=2clt | SCENE= }} | {{STRUCTURE_2clt| PDB=2clt | SCENE= }} | ||
==Structure== | ==Structure== | ||
The Structure of MMP-1 and all other members of the Metalloproteinase family for that matter are formed from three domains. The structure comprises of the N-terminal catalytic domain, the linker region and the C-terminal hemopexin domain. The structure of human MMP-1 was determined with X-Ray Crystallography at a resolution of 2.67A to have two monomers (chains A and B). The catalytic domain of one monomer contacts the hemopexin domain of the other monomer. An interesting observation that has been noted is that the contact site used by the two monomers in the asymmetric unit to form the dimer is not the same as the dimerization site observed in the structure of the MMP-9 hemopexin domain. This difference shows that not all members of the Matrix Metalloproteinase family behave the same in their dimerization processes. Another interesting feature about the protein is that <scene name='Sandbox_Reserved_478/Hydrophobic/1'>Hydrophobic regions</scene> can be found within all areas of the protein rather than being located near a certain domain. | The Structure of MMP-1 and all other members of the Metalloproteinase family for that matter are formed from three domains. The structure comprises of the N-terminal catalytic domain, the linker region and the C-terminal hemopexin domain. The structure of human MMP-1 was determined with X-Ray Crystallography at a resolution of 2.67A to have two monomers (chains A and B).<ref name="lyer">Shalini Iyer, Robert Visse, Hideaki Nagase, K. Ravi Acharya, Crystal Structure of an Active Form of Human MMP-1, Journal of Molecular Biology, Volume 362, Issue 1, 8 September 2006, Pages 78-88, ISSN 0022-2836, 10.1016/j.jmb.2006.06.079.</ref> The catalytic domain of one monomer contacts the hemopexin domain of the other monomer. An interesting observation that has been noted is that the contact site used by the two monomers in the asymmetric unit to form the dimer is not the same as the dimerization site observed in the structure of the MMP-9 hemopexin domain. This difference shows that not all members of the Matrix Metalloproteinase family behave the same in their dimerization processes. Another interesting feature about the protein is that <scene name='Sandbox_Reserved_478/Hydrophobic/1'>Hydrophobic regions</scene> can be found within all areas of the protein rather than being located near a certain domain. | ||
===Catalytic Domain=== | ===Catalytic Domain=== | ||