A helping hand for collagenases: the haemopexin-like domain (Q28275184)

Specific degradation of the collagen molecule by tadpole collagenolytic enzyme

Europe PubMed Central

title

A helping hand for collagenases: the haemopexin-like domain (English)

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author name string

W Bode

series ordinal

1

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language of work or name

English

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publication date

15 June 1995

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published in

Structure

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volume

3

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issue

6

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page(s)

527-30

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cites work

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Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller

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1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin

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The matrix-degrading metalloproteinases

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The matrix metalloproteinases and their inhibitors

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Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

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Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases

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Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor

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The NMR structure of the inhibited catalytic domain of human stromelysin–1

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Structure of human neutrophil collagenase reveals large S1′ specificity pocket

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Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases

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First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases

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Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'

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The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: a possible role for the C-terminal domain

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Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation

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Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms

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Fragmentation of human polymorphonuclear-leucocyte collagenase

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Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity

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The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

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Homology of placental protein 11 and pea seed albumin 2 with vitronectin

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An internal cysteine plays a role in the maintenance of the latency of human fibroblast collagenase.

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

8590012

1 reference

Consolidated OpenCitations Corpus – April 2017