1ESL

INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS

Summary for 1ESL

• Entry DOI: 10.2210/pdb1esl/pdb
• Descriptor: HUMAN E-SELECTIN, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: cell adhesion protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single-pass type I membrane protein: P16581
• Total number of polymer chains: 1
• Total formula weight: 18796.96

Authors

Graves, B.J.,Crowther, R.L. (deposition date: 1994-06-03, release date: 1994-08-31, Last modification date: 2024-10-16)

Primary citation

Graves, B.J.,Crowther, R.L.,Chandran, C.,Rumberger, J.M.,Li, S.,Huang, K.S.,Presky, D.H.,Familletti, P.C.,Wolitzky, B.A.,Burns, D.K.
Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains.
Nature, 367:532-538, 1994

PubMed Abstract: The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.

PubMed: 7509040
DOI: 10.1038/367532a0

Experimental method

X-RAY DIFFRACTION (2 Å)