Sandbox Reserved 478

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Matrix Metalloproteinase 1(MMP1) also known as Interstitial collagenase is a zinc-dependent protease that degrades extracellular matrix proteins. Collagenases are enzymes, which cleave bonds in collagen. MMP1 belongs to the Matrix Metalloproteinase (MMP) family, which are involved in the regulation of cell-matrix composition by the breakdown of the extracellular matrix in normal physiological processes. These physiological processes many include disease activities such as arthritis and metastasis as well as normal human reproduction and embryonic development. StructureStructure 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. Catalytic DomainCatalytic Domain klklm lkm lkm Linker RegionLinker Region asdflkafalkfna;lkdf adfa fa fa Hemopexin-like DomainHemopexin-like Domain adlskflam adfafdaf afa f Mechanism of ActionMechanism of Action sdfglkmsdfsd fasdf a sdf asf ads ff Medical ImplicationsMedical Implications lkmlml;kmlm ReferencesReferences