1GXD
proMMP-2/TIMP-2 complex
Summary for 1GXD
| Entry DOI | 10.2210/pdb1gxd/pdb |
| Related | 1BR9 1CK7 1CXW 1EAK 1GEN 1J7M 1KS0 1RTG 2TMP |
| Descriptor | 72 KDA TYPE IV COLLAGENASE, METALLOPROTEINASE INHIBITOR 2, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, metalloprotease, zymogen, collagen degradation, extracellular matrix, gelatinase a, matrix metalloproteinase 2, proteinase inhibitor |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 186090.81 |
| Authors | Morgunova, E.,Tuuttila, A.,Bergmann, U.,Tryggvason, K. (deposition date: 2002-04-02, release date: 2002-07-09, Last modification date: 2024-10-23) |
| Primary citation | Morgunova, E.,Tuuttila, A.,Bergmann, U.,Tryggvason, K. Structural Insight Into the Complex Formation of Latent Matrix Metalloproteinase 2 with Tissue Inhibitor of Metalloproteinase 2 Proc.Natl.Acad.Sci.USA, 99:7414-, 2002 Cited by PubMed Abstract: Matrix metalloproteinases (MMPs) are a family of multidomain enzymes involved in the physiological degradation of connective tissue, as well as in pathological states such as tumor invasion and arthritis. Apart from transcriptional regulation, MMPs are controlled by proenzyme activation and a class of specific tissue inhibitors of metalloproteinases (TIMPs) that bind to the catalytic site. TIMP-2 is a potent inhibitor of MMPs, but it has also been implicated in a unique cell surface activation mechanism of latent MMP-2/gelatinase A/type IV collagenase (proMMP-2), through its binding to the hemopexin domain of proMMP-2 on the one hand and to a membrane-type MMP activator on the other. The present crystal structure of the human proMMP-2/TIMP-2 complex reveals an interaction between the hemopexin domain of proMMP-2 and the C-terminal domain of TIMP-2, leaving the catalytic site of MMP-2 and the inhibitory site of TIMP-2 distant and spatially isolated. The interfacial contact of these two proteins is characterized by two distinct binding regions composed of alternating hydrophobic and hydrophilic interactions. This unique structure provides information for how specificity for noninhibitory MMP/TIMP complex formation is achieved. PubMed: 12032297DOI: 10.1073/PNAS.102185399 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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