Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZDY

Integrin alphaIIB beta3 headpiece and RGD peptide complex

Summary for 3ZDY
Entry DOI10.2210/pdb3zdy/pdb
Related3ZDX 3ZDZ 3ZE0 3ZE1 3ZE2
DescriptorINTEGRIN ALPHA-IIB, MAGNESIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (12 entities in total)
Functional Keywordscell adhesion-immune system-peptide complex, cell adhesion, cell adhesion/immune system/peptide
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationMembrane; Single-pass type I membrane protein: P08514
Cell membrane ; Single- pass type I membrane protein : P05106
Total number of polymer chains10
Total formula weight303822.63
Authors
Zhu, J.H.,Zhu, J.Q.,Springer, T.A. (deposition date: 2012-12-03, release date: 2013-06-05, Last modification date: 2024-10-23)
Primary citationZhu, J.,Zhu, J.,Springer, T.A.
Complete Integrin Headpiece Opening in Eight Steps.
J.Cell Biol., 201:1053-, 2013
Cited by
PubMed Abstract: Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conformations of the αIIbβ3 integrin headpiece. Starting from the closed βI domain conformation, we saw six intermediate βI conformations and finally the fully open βI with the hybrid domain swung out in the crystal lattice. The β1-α1 backbone that hydrogen bonds to the Asp side chain of RGD was the first element to move followed by adjacent to metal ion-dependent adhesion site Ca(2+), α1 helix, α1' helix, β6-α7 loop, α7 helix, and hybrid domain. We define in atomic detail how conformational change was transmitted over long distances in integrins, 40 Å from the ligand binding site to the opposite end of the βI domain and 80 Å to the far end of the hybrid domain. During these movements, RGD slid in its binding groove toward αIIb, and its Arg side chain became ordered. RGD concentration requirements in soaking suggested a >200-fold higher affinity after opening. The thermodynamic cycle shows how higher affinity pays the energetic cost of opening.
PubMed: 23798730
DOI: 10.1083/JCB.201212037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon