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| <StructureSection load='1g1r' size='450' side='right' caption='Structure of P-selectin EGF domain complex with tetrasaccharide and Ca+2 ion (green) (PDB entry [[1g1r]])' scene='55/552185/Cv/1'> | | <StructureSection load='1g1r' size='350' side='right' caption='Structure of P-selectin EGF domain complex with tetrasaccharide and Ca+2 ion (green) (PDB entry [[1g1r]])' scene='55/552185/Cv/1'> |
| == Function == | | == Function == |
| '''Selectin''' or '''CD62''' are cell adhesion molecules which bind sugar moieties and thus are regarded as lectins. The structure of selectin consists of extracellular calcium-dependent lectin domain, an EGF-like domain and a number of concensus repeat units, a transmembranal domain and a intracellular domain<ref>PMID:7542213</ref>. Three types of selectins are found:<br /> | | '''Selectin''' or '''CD62''' are cell adhesion molecules which bind sugar moieties and thus are regarded as lectins. The structure of selectin consists of extracellular calcium-dependent lectin domain, an EGF-like domain and a number of concensus repeat units, a transmembranal domain and a intracellular domain<ref>PMID:7542213</ref>. Three types of selectins are found:<br /> |
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| **[[3cfw]] – hCD62L EGF domain <br /> | | **[[3cfw]] – hCD62L EGF domain <br /> |
| | **[[5vc1]] – hCD62L EGF domain (mutant)<br /> |
| **[[2lgf]] – hCD62L calmodulin-binding domain + calmodulin<br /> | | **[[2lgf]] – hCD62L calmodulin-binding domain + calmodulin<br /> |
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Revision as of 18:27, 17 September 2018
| Function
Selectin or CD62 are cell adhesion molecules which bind sugar moieties and thus are regarded as lectins. The structure of selectin consists of extracellular calcium-dependent lectin domain, an EGF-like domain and a number of concensus repeat units, a transmembranal domain and a intracellular domain[1]. Three types of selectins are found:
- E-selectin found in endothelial cells
- L-selectin found in leukocytes
- P-selectin found in platelets.
Relevance
Selectins are involved in inflammation processes. The L-selectins on the surface of leukocytes bind to carbohydrates causing the cells to roll along the blood vessel walls, slowing their motion and enabling them to enter the site of infection[2]. E-selectin levels correlate with disease activity in psoriasis patients[3]. L-selectin levels correlate with disease activity in type I diabetes[4].
Structural insight
The tetrasaccharide binding interactions to P-selectin are electrostatic[5]. Ca coordination site.
- ↑ Tedder TF, Steeber DA, Chen A, Engel P. The selectins: vascular adhesion molecules. FASEB J. 1995 Jul;9(10):866-73. PMID:7542213
- ↑ Ley K. The role of selectins in inflammation and disease. Trends Mol Med. 2003 Jun;9(6):263-8. PMID:12829015
- ↑ Szepietowski J, Wasik F, Bielicka E, Nockowski P, Noworolska A. Soluble E-selectin serum levels correlate with disease activity in psoriatic patients. Clin Exp Dermatol. 1999 Jan;24(1):33-6. PMID:10233646
- ↑ Kretowski A, Gillespie KM, Bingley PJ, Kinalska I. Soluble L-selectin levels in type I diabetes mellitus: a surrogate marker for disease activity? Immunology. 2000 Feb;99(2):320-5. PMID:10692053
- ↑ Somers WS, Tang J, Shaw GD, Camphausen RT. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Cell. 2000 Oct 27;103(3):467-79. PMID:11081633
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3D structures of selectin
Updated on 17-September-2018
{"openlevels":0}
- P-selectin
- 1fsb – hCD62P EGF domain – human - NMR
- 1g1q – hCD62P EGF domain
- 1g1r – hCD62P EGF domain + tetrasaccharide
- 1g1s – hCD62P EGF domain +P-selectin glycoprotein ligand peptide
- 4gxb – hCD62P intracellular domain + sorting nexin-17
- L-selectin
- 3cfw – hCD62L EGF domain
- 5vc1 – hCD62L EGF domain (mutant)
- 2lgf – hCD62L calmodulin-binding domain + calmodulin
- E-selectin
- 1esl – hCD62E EGF domain
- 1g1t – hCD62E EGF domain + tetrasaccharide
- 4c16 – hCD62 EGF+SCR domains + antagonist
- 4csy – hCD62 EGF+SCR domains + ligand
References
