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3HO3

Crystal structure of Hedgehog-interacting protein (HHIP)

Summary for 3HO3
Entry DOI10.2210/pdb3ho3/pdb
Related3HO4 3HO5
DescriptorHedgehog-interacting protein (1 entity in total)
Functional Keywordsreceptor ectodomain, six-bladed-propeller domain, egf domain, disulfide bond, cell membrane, egf-like domain, glycoprotein, membrane, secreted, signaling protein
Biological sourceHomo sapiens (human)
Cellular locationCell membrane; Peripheral membrane protein (By similarity). Isoform 2: Cytoplasm (Probable): Q96QV1
Total number of polymer chains1
Total formula weight54087.25
Authors
Bosanac, I.,Hymowitz, S.G. (deposition date: 2009-06-01, release date: 2009-06-23, Last modification date: 2024-10-30)
Primary citationBosanac, I.,Maun, H.R.,Scales, S.J.,Wen, X.,Lingel, A.,Bazan, J.F.,de Sauvage, F.J.,Hymowitz, S.G.,Lazarus, R.A.
The structure of SHH in complex with HHIP reveals a recognition role for the Shh pseudo active site in signaling.
Nat.Struct.Mol.Biol., 16:691-697, 2009
Cited by
PubMed Abstract: Hedgehog (Hh) signaling is crucial for many aspects of embryonic development, whereas dysregulation of this pathway is associated with several types of cancer. Hedgehog-interacting protein (Hhip) is a surface receptor antagonist that is equipotent against all three mammalian Hh homologs. The crystal structures of human HHIP alone and bound to Sonic hedgehog (SHH) now reveal that HHIP is comprised of two EGF domains and a six-bladed beta-propeller domain. In the complex structure, a critical loop from HHIP binds the pseudo active site groove of SHH and directly coordinates its Zn2+ cation. Notably, sequence comparisons of this SHH binding loop with the Hh receptor Patched (Ptc1) ectodomains and HHIP- and PTC1-peptide binding studies suggest a 'patch for Patched' at the Shh pseudo active site; thus, we propose a role for Hhip as a structural decoy receptor for vertebrate Hh.
PubMed: 19561609
DOI: 10.1038/nsmb.1632
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

243083

数据于2025-10-15公开中

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