1NLO	Complex (Transferase Peptide)	date	Aug 04, 1996
title	Structure Of Signal Transduction Protein, Nmr, Minimized Average Structure
authors	S.Feng, T.M.Kapoor, F.Shirai, A.P.Combs, S.L.Schreiber
compound		source
Molecule: C-Src Chain: C Fragment: Sh3 Domain Ec: 2.7.1.112 Engineered: Yes		Expression_system: Gst-Fusion Expression_system_plasmid: Pgex-2t Expression_system_gene: Chicken
Molecule: Nl1 (Mn7-Mn2-Mn1-Plpplp) Chain: N Engineered: Yes Other_details: Ligand Nl1 Contains Non-Peptide Elements		Synthetic: Yes
method	NMR, Minimized Average Structure
ligand	ACE, MN7, MN2, MN1, NH2	enzyme	Protein-tyrosine kinase. Tyrosylprotein kinase. Protein kinase (tyrosine). Hydroxyaryl-protein kinase. Ectoprotein kinase. Gene lck protein kinase. Gene lck tyrosine kinase. Hydroxyaryl-protein kinase. Insulin receptor protein-tyrosine kinase. IRK. JAK protein tyrosine kinase. Protein p56lck kinase (phosphorylating):), protein (tyrosine) kinase (phosphorylating). Lck tyrosine kinase. Nonreceptor protein tyrosine kinase. P56lck protein tyrosine kinase. P56lck tyrosine kinase. P56lck protein kinase. P56lck kinase. Phosphotyrosyl-protein kinase. Protein p56c-lck kinase. Protein p56lck tyrosine kinase. Protein tyrosine kinase lck. Protein tyrosine kinase p56lck. Protein tyrosine kinase pp56lck. Protein kinase p56lck. Protein tyrosine kinase. Protein kinase (tyrosine-phosphorylating). Protein kinase p56-LCK. Protein kinase Lck. Receptor-activated Janus kinase. Tyrosine kinase lck. Tyrosine protein kinase p56lck. Tyrosine kinase p56lck. Tyrosine kinase. Tyrosine phosphokinase. Tyrosine protein kinase. Tyrosine-specific protein kinase. Tyrosylprotein kinase. V-fps protein-tyrosine kinase. Transferase E.C.2.7.1.112
similarity	Src subfamily. Belongs to the tyr family of protein kinases. Contains 1 sh2 domain. Contains 1 SH3 domain.
catalytic activ.	Atp + a protein tyrosine = adp + protein tyrosine phosphate.
post-translat. modifications	Phosphorylated on tyr-526 by c-src kinase (csk). The phosphorylated tail interacts with the sh2 domain thereby repressing kinase activity (by similarity).
enzyme regulation	It can also be activated by point mutations as well as by truncations at the c-terminal end or by other mutations. Becomes activated when its major tyrosine phosphorylation site is not phosphorylated.
genes	V-SRC (A. sarcoma); V-SRC (A. sarcoma); SRC (G. gallus); V-ABL (F. sarcoma); ABL, ABL1, AGMX1, ATK, BEK, BPK, BTK, CSK, ERBB2, ERBB3, FGFBR, FGFR1, FGFR2, FLG, FLT2, FYN, GRB1, HCK, HER2, HER3, IGF1R, INSR, JTK7, KSAM, LCK, NEU, NGL, PIK3R1, SRC, SRC1, SYK (H. sapiens); NEF (H. immunodeficiency); NEF (H. immunodeficiency); ABL1, ABL, BLK, EFNB2, ELF2, EMT, EPHB2, EPL5, EPLG5, EPTH3, HTKL, ITK, LERK5, NUK, SEK3, TLK, TSK (M. musculus); CSK (R. norvegicus); V-SRC (R. sarcoma)
function	The function of pp60-c-src is unknown. It is expressed to high levels, and with a high degree of kinase activity, in certain fully differentiated cells such as neurons, platelets and macrophages. This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.
disease	Leukemia,Philadelphia chromosome-positive,resistant to imatinib Agammaglobulinemia,type 1,X-linked XLA and isolated growthhormone deficiency Antley-Bixler syndrome Apert syndrome Beare-Stevenson cutis gyrata syndrome Craniofacial-skeletal-dermatologic dysplasia Craniosynostosis,nonspecific Crouzon syndrome Gastric cancer,somatic Jackson-Weiss syndrome Pfeiffer syndrome Saethre-Chotzen syndrome Jackson-Weiss sydnrome Kallmann syndrome 2 Ichthyosis vulgaris Diabetes mellitus,insulin-resistant,with acanthosis nigricans Leprechaunism Rabson-Mendenhall syndrome SCID due to LCK deficiency Sialidosis,type I Sialidosis,type II Colon cancer,advanced

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (28 Kb) [Save to disk] LPC: Ligand-Protein Contacts for 1NLO CSU: Contacts of Structural Units for 1NLO Likely Quarternary Molecular Structure file(s) for 1NLO Retrieve 1NLO in mmCIF format [Save to disk]

View 1NLO in 3D

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Visual 3D analysis of 1NLO

STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure. Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges. GRASS (Graphical Representation and Analysis of Structure Server) Cartoon representation from PDB Cartoon

View 1NLO in 2D

Topology of domains/folds: Chain: C from TOPS (The Atlas of protein topology cartoons )

Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Genome occurence of 1NLO's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1nloc_, region C: [rasmolscript] [script source] Fold representative 1nlo from FSSP and Dali (Families of Structurally Similar Proteins) Domain Definition for 1nlo from 3Dee ( The Database of Protein Domain Definitions ) Class (fold), Architecture (subfold), Topology, Homologous superfamily: CATH Summaries and structural analyses of PDB data files: PDBSum

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1nlo_C] [1nlo_N] SWISS-PROT database: [SRC_AVISR] [SRC_CHICK] Domain organization of [SRC_AVISR] [SRC_CHICK] by SWISSPFAM Domain found in 1NLO: [SH3 ] by SMART Conserved protein region description, domain view and alignment from family SH3 (PF00018) of Pfam. Alignments of the sequence of 1NLO with the sequences similar proteins can be viewed for classification [SRC_AVISR] [SRC_CHICK] at ProtoMap. Click on "Neighbors List", then on the "See Alignments" button below the list. A sequence distance tree ("phylogenetic tree") can be viewed for 1ACL's classification [SRC_AVISR] [SRC_CHICK] at ProtoMap. Click on the Cluster number.

Other resources with information on 1NLO

InterPro: IPR000980 , IPR001452 , IPR001245 , IPR000719 PDBREPORT (protein verification by WHAT_CHECK procedures) MMDB (Entrez's Structure Database)

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