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The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function
Author(s) -
Gohlke Ulrich,
Gomis-Rüth Franz-Xaver,
Crabbe Thomas,
Murphy Gillian,
Docherty Andrew J.P.,
Bode Wolfram
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01435-7
Subject(s) - gelatinase , matrix metalloproteinase , chemistry , collagenase , biophysics , topology (electrical circuits) , biochemistry , biology , enzyme , mathematics , combinatorics
In common with most other matrix metalloproteinases, gelatinase A has a non‐catalytic C‐terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 Å resolution, which was refined to an R value of 17.9%. This structure has a disc‐like shape, with the chain folded into a β‐propeller structure that has pseudo four‐fold symmetry. Although the topology and the side‐chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C‐terminal domain to bind to natural inhibitor TIMP‐2.