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1yh3
From Proteopedia
| 1yh3, resolution 1.91Å () | |||||||||
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| Gene: | CD38 (Homo sapiens) | ||||||||
| Activity: | NAD(+) nucleosidase, with EC number 3.2.2.5 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal structure of human CD38 extracellular domain
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1yh3 is a 2 chain structure of ADP-ribosyl cyclase 1 and Cluster of Differentiation 38 with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q. Crystal structure of human CD38 extracellular domain. Structure. 2005 Sep;13(9):1331-9. PMID:16154090 doi:10.1016/j.str.2005.05.012
