1yh3: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] </span> | ||
|GENE= CD38 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CD38 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yh3 OCA], [http://www.ebi.ac.uk/pdbsum/1yh3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yh3 RCSB]</span> | |||
}} | }} | ||
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[[Category: cell surface receptor]] | [[Category: cell surface receptor]] | ||
[[Category: membrane association]] | [[Category: membrane association]] | ||
[[Category: parallel beta | [[Category: parallel beta sheets,two domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:07:08 2008'' | ||
Revision as of 01:07, 31 March 2008
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| , resolution 1.91Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CD38 (Homo sapiens) | ||||||
| Activity: | NAD(+) nucleosidase, with EC number 3.2.2.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human CD38 extracellular domain
OverviewOverview
Human CD38 is a multifunctional protein involved in diverse functions. As an enzyme, it is responsible for the synthesis of two Ca2+ messengers, cADPR and NAADP; as an antigen, it is involved in regulating cell adhesion, differentiation, and proliferation. Besides, CD38 is a marker of progression of HIV-1 infection and a negative prognostic marker of B-CLL. We have determined the crystal structure of the soluble extracellular domain of human CD38 to 1.9 A resolution. The enzyme's overall topology is similar to the related proteins CD157 and the Aplysia ADP-ribosyl cyclase, except with large structural changes at the two termini. The extended positively charged N terminus has lateral associations with the other CD38 molecule in the crystallographic asymmetric unit. The analysis of the CD38 substrate binding models revealed two key residues that may be critical in controlling CD38's multifunctionality of NAD hydrolysis, ADP-ribosyl cyclase, and cADPR hydrolysis activities.
About this StructureAbout this Structure
1YH3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human CD38 extracellular domain., Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q, Structure. 2005 Sep;13(9):1331-9. PMID:16154090
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