2zg2
From Proteopedia
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'''Crystal Structure of Two N-terminal Domains of Native Siglec-5''' | '''Crystal Structure of Two N-terminal Domains of Native Siglec-5''' | ||
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[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
[[Category: Zhuravleva, M A.]] | [[Category: Zhuravleva, M A.]] | ||
| - | [[Category: | + | [[Category: C2-set]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Ig-like domain]] |
| - | [[Category: | + | [[Category: Immune system/carbohydrate binding protein complex]] |
| - | [[Category: | + | [[Category: Immunoglobulin domain]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Membrane]] |
| - | [[Category: | + | [[Category: Polymorphism]] |
| - | [[Category: | + | [[Category: Sialic acid]] |
| - | [[Category: | + | [[Category: Siglec-5 inhibitory receptor]] |
| - | [[Category: | + | [[Category: Transmembrane]] |
| - | [[Category: | + | [[Category: Two-domain structure]] |
| - | [[Category: | + | [[Category: V-set]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:12:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:12, 4 May 2008
Crystal Structure of Two N-terminal Domains of Native Siglec-5
Overview
Sialic acid (Sia) Ig-like binding lectins are important mediators of recognition and signaling events among myeloid cells. To investigate the molecular mechanism underlying sialic acid Ig-like lectin (Siglec) functions, we determined the crystal structure of the two N-terminal extracellular domains of human myeloid cell inhibitory receptor Siglec-5 (CD170) and its complexes with two sialylated carbohydrates. The native structure revealed an unusual conformation of the CC' ligand specificity loop and a unique interdomain disulfide bond. The alpha(2,3)- and alpha(2,6)-sialyllactose complexed structures showed a conserved Sia recognition motif that involves both Arg124 and a portion of the G-strand in the V-set domain forming beta-sheet-like hydrogen bonds with the glycerol side chain of the Sia. Only few protein contacts to the subterminal sugars are observed and mediated by the highly variable GG' linker and CC' loop. These structural observations, in conjunction with surface plasmon resonance binding assays, provide mechanistic insights into linkage-dependent Siglec carbohydrate recognition and suggest that Siglec-5 and other CD33-related Siglec receptors are more promiscuous in sialoglycan recognition than previously understood.
About this Structure
2ZG2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural implications of Siglec-5-mediated sialoglycan recognition., Zhuravleva MA, Trandem K, Sun PD, J Mol Biol. 2008 Jan 11;375(2):437-47. Epub 2007 Oct 11. PMID:18022638 Page seeded by OCA on Sun May 4 20:12:12 2008
Categories: Homo sapiens | Single protein | Sun, P D. | Zhuravleva, M A. | C2-set | Cell adhesion | Glycoprotein | Ig-like domain | Immune system/carbohydrate binding protein complex | Immunoglobulin domain | Lectin | Membrane | Polymorphism | Sialic acid | Siglec-5 inhibitory receptor | Transmembrane | Two-domain structure | V-set
