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PDBsum entry 1ld2

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Cell cycle PDB id
1ld2
Contents
Protein chain
303 a.a.

References listed in PDB file
Key reference
Title Structural effects of monovalent anions on polymorphic lysozyme crystals.
Authors M.C.Vaney, I.Broutin, P.Retailleau, A.Douangamath, S.Lafont, C.Hamiaux, T.Prangé, A.Ducruix, M.Riès-Kautt.
Ref. Acta Crystallogr D Biol Crystallogr, 2001, 57, 929-940. [DOI no: 10.1107/S0907444901004504]
PubMed id 11418760
Abstract
Understanding direct salt effects on protein crystal polymorphism is addressed by comparing different crystal forms (triclinic, monoclinic, tetragonal and orthorhombic) for hen, turkey, bob white quail and human lysozymes. Four new structures of hen egg-white lysozyme are reported: crystals grown in the presence of NapTS diffracted to 1.85 A, of NaI to 1.6 A, of NaNO(3) to 1.45 A and of KSCN to 1.63 A. These new structures are compared with previously published structures in order to draw a mapping of the surface of different lysozymes interacting with monovalent anions, such as nitrate, chloride, iodide, bromide and thiocyanate. An analysis of the structural sites of these anions in the various lysozyme structures is presented. This study shows common anion sites whatever the crystal form and the chemical nature of anions, while others seem specific to a given geometry and a particular charge environment induced by the crystal packing.
Figure 4.
Figure 4 R.m.s. deviations versus the sequence number between the two independent molecules of the HEWL/NaI monoclinic structure showing the non-equivalence of loops 65-75.
Figure 6.
Figure 6 All anionic sites (red numbers) aligned on the lysozyme sequence. The unique sites are labelled according to the chemical formula of the anion taken from the corresponding PDB file.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 929-940) copyright 2001.
Secondary reference #1
Title Transcript mapping in a 46-Kb sequenced region at the core of 12q13.3 amplification in human cancers.
Authors A.G.Elkahloun, D.B.Krizman, Z.Wang, T.A.Hofmann, B.Roe, P.S.Meltzer.
Ref. Genomics, 1997, 42, 295-301. [DOI no: 10.1006/geno.1997.4727]
PubMed id 9192850
Full text Abstract
Secondary reference #2
Title Homology probing: identification of cdna clones encoding members of the protein-Serine kinase family.
Author S.K.Hanks.
Ref. Proc Natl Acad Sci U S A, 1987, 84, 388-392. [DOI no: 10.1073/pnas.84.2.388]
PubMed id 2948189
Full text Abstract
Secondary reference #3
Title Coamplification of the cdk4 gene with mdm2 and gli in human sarcomas.
Authors Z.A.Khatib, H.Matsushime, M.Valentine, D.N.Shapiro, C.J.Sherr, A.T.Look.
Ref. Cancer Res, 1993, 53, 5535-5541.
PubMed id 8221695
Abstract
Secondary reference #4
Title A p16ink4a-Insensitive cdk4 mutant targeted by cytolytic t lymphocytes in a human melanoma.
Authors T.Wölfel, M.Hauer, J.Schneider, M.Serrano, C.Wölfel, E.Klehmann-Hieb, E.De plaen, T.Hankeln, K.H.Meyer zum büschenfelde, D.Beach.
Ref. Science, 1995, 269, 1281-1284. [DOI no: 10.1126/science.7652577]
PubMed id 7652577
Full text Abstract
Secondary reference #5
Title Germline mutations in the p16ink4a binding domain of cdk4 in familial melanoma.
Authors L.Zuo, J.Weger, Q.Yang, A.M.Goldstein, M.A.Tucker, G.J.Walker, N.Hayward, N.C.Dracopoli.
Ref. Nat Genet, 1996, 12, 97-99.
PubMed id 8528263
Abstract
Secondary reference #6
Title Structural basis of inhibition of cdk-Cyclin complexes by ink4 inhibitors.
Authors P.D.Jeffrey, L.Tong, N.P.Pavletich.
Ref. Genes Dev, 2000, 14, 3115-3125.
PubMed id 11124804
Abstract
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