2JXY
Solution structure of the hemopexin-like domain of MMP12
Summary for 2JXY
| Entry DOI | 10.2210/pdb2jxy/pdb |
| NMR Information | BMRB: 7414,7415,15578 |
| Descriptor | Macrophage metalloelastase, CALCIUM ION (2 entities in total) |
| Functional Keywords | b-sheet hydrophobic core, calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P39900 |
| Total number of polymer chains | 1 |
| Total formula weight | 23240.53 |
| Authors | Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M. (deposition date: 2007-12-01, release date: 2008-05-27, Last modification date: 2024-11-13) |
| Primary citation | Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Mylonas, E.,Svergun, D.I. Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12 J.Am.Chem.Soc., 130:7011-7021, 2008 Cited by PubMed Abstract: The proteolytic activity of matrix metalloproteinases toward extracellular matrix components (ECM), cytokines, chemokines, and membrane receptors is crucial for several homeostatic and pathological processes. Active MMPs are a family of single-chain enzymes (23 family members in the human genome), most of which constituted by a catalytic domain and by a hemopexin-like domain connected by a linker. The X-ray structures of MMP-1 and MMP-2 suggest a conserved and well-defined spatial relationship between the two domains. Here we present structural data for MMP-12, suitably stabilized against self-hydrolysis, both in solution (NMR and SAXS) and in the solid state (X-ray), showing that the hemopexin-like and the catalytic domains experience conformational freedom with respect to each other on a time scale shorter than 10(-8) s. Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs. PubMed: 18465858DOI: 10.1021/ja710491y PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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