2LLP
Solution structure of a THP type 1 alpha 1 collagen fragment (772-786)
Summary for 2LLP
| Entry DOI | 10.2210/pdb2llp/pdb |
| NMR Information | BMRB: 18083 |
| Descriptor | Collagen alpha-1(I) chain (1 entity in total) |
| Functional Keywords | triple helical peptide, structural protein, contractile protein, structural genomics, structural proteomics in europe 2, spine-2 |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted, extracellular space, extracellular matrix (By similarity): P02452 |
| Total number of polymer chains | 3 |
| Total formula weight | 4973.68 |
| Authors | Bertini, I.,Fragai, M.,Luchinat, C.,Melikian, M.,Toccafondi, M.,Lauer, J.L.,Fields, G.B.,Structural Proteomics in Europe 2 (SPINE-2) (deposition date: 2011-11-15, release date: 2012-05-30, Last modification date: 2024-05-01) |
| Primary citation | Bertini, I.,Fragai, M.,Luchinat, C.,Melikian, M.,Toccafondi, M.,Lauer, J.L.,Fields, G.B. Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis. J.Am.Chem.Soc., 134:2100-2110, 2012 Cited by PubMed Abstract: The proteolysis of collagen triple-helical structure (collagenolysis) is a poorly understood yet critical physiological process. Presently, matrix metalloproteinase 1 (MMP-1) and collagen triple-helical peptide models have been utilized to characterize the events and calculate the energetics of collagenolysis via NMR spectroscopic analysis of 12 enzyme-substrate complexes. The triple-helix is bound initially by the MMP-1 hemopexin-like (HPX) domain via a four amino acid stretch (analogous to type I collagen residues 782-785). The triple-helix is then presented to the MMP-1 catalytic (CAT) domain in a distinct orientation. The HPX and CAT domains are rotated with respect to one another compared with the X-ray "closed" conformation of MMP-1. Back-rotation of the CAT and HPX domains to the X-ray closed conformation releases one chain out of the triple-helix, and this chain is properly positioned in the CAT domain active site for subsequent hydrolysis. The aforementioned steps provide a detailed, experimentally derived, and energetically favorable collagenolytic mechanism, as well as significant insight into the roles of distinct domains in extracellular protease function. PubMed: 22239621DOI: 10.1021/ja208338j PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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