1YH3

Crystal structure of human CD38 extracellular domain

Summary for 1YH3

• Entry DOI: 10.2210/pdb1yh3/pdb
• Descriptor: ADP-ribosyl cyclase 1 (2 entities in total)
• Functional Keywords: parallel beta sheets, two domains, membrane association, cell surface receptor, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type II membrane protein: P28907
• Total number of polymer chains: 2
• Total formula weight: 59299.27

Authors

Liu, Q.,Kriksunov, I.A.,Graeff, R.,Munshi, C.,Lee, H.C.,Hao, Q. (deposition date: 2005-01-06, release date: 2005-09-27, Last modification date: 2024-10-30)

Primary citation

Liu, Q.,Kriksunov, I.A.,Graeff, R.,Munshi, C.,Lee, H.C.,Hao, Q.
Crystal structure of human CD38 extracellular domain.
Structure, 13:1331-1339, 2005

PubMed Abstract: 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.

PubMed: 16154090
DOI: 10.1016/j.str.2005.05.012

Experimental method

X-RAY DIFFRACTION (1.91 Å)