3mvi: Difference between revisions
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{{STRUCTURE_3mvi| PDB=3mvi | SCENE= }} | {{STRUCTURE_3mvi| PDB=3mvi | SCENE= }} | ||
===Crystal structure of holo mADA at 1.6 A resolution=== | ===Crystal structure of holo mADA at 1.6 A resolution=== | ||
{{ABSTRACT_PUBMED_20815357}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE]] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). | |||
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020815357</ref><ref group="xtra">PMID:009622483</ref><references group="xtra"/><references/> | ||
[[Category: Adenosine deaminase]] | [[Category: Adenosine deaminase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: Niu, W.]] | [[Category: Niu, W.]] | ||
[[Category: Shu, Q.]] | [[Category: Shu, Q.]] | ||
[[Category: Adenosine deaminase]] | |||
[[Category: Hydrolase]] | |||
Revision as of 23:52, 17 April 2013
Crystal structure of holo mADA at 1.6 A resolutionCrystal structure of holo mADA at 1.6 A resolution
Template:ABSTRACT PUBMED 20815357
FunctionFunction
[ADA_MOUSE] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
About this StructureAbout this Structure
3mvi is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Niu W, Shu Q, Chen Z, Mathews S, Di Cera E, Frieden C. The Role of Zn(2+) on the Structure and Stability of Murine Adenosine Deaminase (dagger). J Phys Chem B. 2010 Sep 3. PMID:20815357 doi:10.1021/jp106041v
- ↑ Wang Z, Quiocho FA. Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity. Biochemistry. 1998 Jun 9;37(23):8314-24. PMID:9622483 doi:10.1021/bi980324o