1yh3

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{{STRUCTURE_1yh3| PDB=1yh3 | SCENE= }}
{{STRUCTURE_1yh3| PDB=1yh3 | SCENE= }}
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'''Crystal structure of human CD38 extracellular domain'''
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===Crystal structure of human CD38 extracellular domain===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16154090 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16154090}}
==About this Structure==
==About this Structure==
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[[Category: Membrane association]]
[[Category: Membrane association]]
[[Category: Parallel beta sheets,two domain]]
[[Category: Parallel beta sheets,two domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:18:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:38:46 2008''

Revision as of 05:38, 29 July 2008

Template:STRUCTURE 1yh3

Crystal structure of human CD38 extracellular domain

Template:ABSTRACT PUBMED 16154090

About this Structure

1YH3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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