1a5i
From Proteopedia
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 12:40, 30 October 2007
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CATALYTIC DOMAIN OF VAMPIRE BAT (DESMODUS ROTUNDUS) SALIVA PLASMINOGEN ACTIVATOR IN COMPLEX WITH EGR-CMK (GLU-GLY-ARG CHLOROMETHYL KETONE)
Overview
The saliva of the blood-eating vampire bat Desmodus rotundus contains, plasminogen activators (PAs) that maintain the fluidity of the prey's, blood by activating plasminogen and dissolving developing fibrin clots. D., rotundus salivary PAs (DSPAs) are composed of evolutionarily conserved, domains reminiscent of human tissue-type PA (tPA), but their catalytic, domain lacks a plasmin-sensitive "activation cleavage site". Despite this, all DSPAs are intrinsically active and enormously stimulated in the, presence of fibrin. The recombinant catalytic domain of DSPAalpha1 has, been crystallized in a covalent complex with Glu-Gly-Arg-chloromethyl, ketone and its structure solved at 2.9 A resolution. The structure is, similar to that of activated two-chain human tPA. Despite its single-chain, ... [(full description)]
About this Structure
1A5I is a [Single protein] structure of sequence from [Desmodus rotundus] with CH2 as [ligand]. Active as [T-plasminogen activator], with EC number [3.4.21.68]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].
Reference
Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage., Renatus M, Stubbs MT, Huber R, Bringmann P, Donner P, Schleuning WD, Bode W, Biochemistry. 1997 Nov 4;36(44):13483-93. PMID:9354616
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