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4TW2

Crystal Structure of SCARB2 in Neural Condition (pH7.5)

Summary for 4TW2
Entry DOI10.2210/pdb4tw2/pdb
Related4TVZ 4TW0
DescriptorScavenger receptor class B member 2, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordslipid binding tunnel, protein binding
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight97291.46
Authors
Dang, M.H.,Wang, X.X.,Rao, Z.H. (deposition date: 2014-06-29, release date: 2015-07-08, Last modification date: 2024-11-06)
Primary citationDang, M.,Wang, X.,Wang, Q.,Wang, Y.,Lin, J.,Sun, Y.,Li, X.,Zhang, L.,Lou, Z.,Wang, J.,Rao, Z.
Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71
Protein Cell, 5:692-703, 2014
Cited by
PubMed Abstract: Unlike the well-established picture for the entry of enveloped viruses, the mechanism of cellular entry of non-enveloped eukaryotic viruses remains largely mysterious. Picornaviruses are representative models for such viruses, and initiate this entry process by their functional receptors. Here we present the structural and functional studies of SCARB2, a functional receptor of the important human enterovirus 71 (EV71). SCARB2 is responsible for attachment as well as uncoating of EV71. Differences in the structures of SCARB2 under neutral and acidic conditions reveal that SCARB2 undergoes a pivotal pH-dependent conformational change which opens a lipid-transfer tunnel to mediate the expulsion of a hydrophobic pocket factor from the virion, a pre-requisite for uncoating. We have also identified the key residues essential for attachment to SCARB2, identifying the canyon region of EV71 as mediating the receptor interaction. Together these results provide a clear understanding of cellular attachment and initiation of uncoating for enteroviruses.
PubMed: 24986489
DOI: 10.1007/s13238-014-0087-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.889 Å)
Structure validation

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数据于2025-06-25公开中

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