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

1QCY

THE CRYSTAL STRUCTURE OF THE I-DOMAIN OF HUMAN INTEGRIN ALPHA1BETA1

Summary for 1QCY
Entry DOI10.2210/pdb1qcy/pdb
DescriptorI-DOMAIN OF INTEGRIN ALPHA1BETA1, MAGNESIUM ION (3 entities in total)
Functional Keywordsdinucleotide binding fold, rossmann fold, cell adhesion
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein: P56199
Total number of polymer chains1
Total formula weight21570.71
Authors
Kankare, J.A.,Salminen, T.A.,Nymalm, Y.,Kaepylae, J.,Heino, J.,Johnson, M.S. (deposition date: 1999-05-12, release date: 2003-09-02, Last modification date: 2024-02-14)
Primary citationNymalm, Y.,Puranen, J.S.,Nyholm, T.K.M.,Kaepylae, J.,Kidron, H.,Pentikaeinen, O.T.,Airenne, T.T.,Heino, J.,Slotte, J.P.,Johnson, M.S.,Salminen, T.A.
Jararhagin-derived RKKH Peptides Induce Structural Changes in a1I Domain of Human Integrin a1b1
J.Biol.Chem., 279:7962-7970, 2004
Cited by
PubMed Abstract: Integrin alpha(1)beta(1) is one of four collagen-binding integrins in humans. Collagens bind to the alphaI domain and in the case of alpha(2)I collagen binding is competitively inhibited by peptides containing the RKKH sequence and derived from the metalloproteinase jararhagin of snake venom from Bothrops jararaca. In alpha(2)I, these peptides bind near the metal ion-dependent adhesion site (MIDAS), where a collagen (I)-like peptide is known to bind; magnesium is required for binding. Published structures of the ligand-bound "open" conformation of alpha(2)I differs significantly from the "closed" conformation seen in the structure of apo-alpha(2)I near MIDAS. Here we show that two peptides, CTRKKHDC and CARKKHDC, derived from jararhagin also bind to alpha(1)I and competitively inhibit collagen I binding. Furthermore, calorimetric and fluorimetric measurements show that the structure of the complex of alpha(1)I with Mg(2+) and CTRKKHDC differs from structure in the absence of peptide. A comparison of the x-ray structure of apo-alpha(1)I ("closed" conformation) and a model structure of the alpha(1)I ("open" conformation) based on the closely related structure of alpha(2)I reveals that the binding site is partially blocked to ligands by Glu(255) and Tyr(285) in the "closed" structure, whereas in the "open" structure helix C is unwound and these residues are shifted, and the "RKKH" peptides fit well when docked. The "open" conformation of alpha(2)I resulting from binding a collagen (I)-like peptide leads to exposure of hydrophobic surface, also seen in the model of alpha(1)I and shown experimentally for alpha(1)I using a fluorescent hydrophobic probe.
PubMed: 14660600
DOI: 10.1074/jbc.M312912200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon