Structural highlights
3hdb is a 2 chain structure with sequence from Deinagkistrodon acutus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.31Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
AaHIV, a P-III-type snake venom metalloproteinase (SVMP), consists of metalloproteinase/disintegrin/cysteine-rich (MDC) domains and is homologous to a disintegrin and metalloproteinase (ADAM) family proteins. Similar to brevilysin H6 and jararhagin, AaHIV can easily autolyse to release a stable protein named acucetin, which contains disintegrin-like and cysteine-rich domains. In this study, we determined the crystal structure of AaHIV and investigated the autolysis mechanism. Based on the structure of AaHIV and the results from docking experiments, we present a new model for target recognition in which two protein molecules form a functional unit, and the DC domain of one molecule is used for target recognition while the M-domain of the other is used for target proteolysis. Our results shed new light on the mechanism of target recognition and processing in ADAM/reprolysin family proteins.
Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM/reprolysin family proteins.,Zhu Z, Gao Y, Zhu Z, Yu Y, Zhang X, Zang J, Teng M, Niu L Biochem Biophys Res Commun. 2009 Aug 14;386(1):159-64. Epub 2009 Jun 6. PMID:19505434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhu Z, Gao Y, Zhu Z, Yu Y, Zhang X, Zang J, Teng M, Niu L. Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM/reprolysin family proteins. Biochem Biophys Res Commun. 2009 Aug 14;386(1):159-64. Epub 2009 Jun 6. PMID:19505434 doi:10.1016/j.bbrc.2009.06.004
